Cellular Membranes

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 An Overview of Membrane Functions

• Compartmentalization (1)
Membranes form continuous sheets
that enclose intracellular
compartments.
• Scaffold for biochemical activities (2)
Membranes provide a framework
that organizes enzymes for effective
interaction.
• Selectively permeable barrier (3)
Membranes allow regulated
exchange of substances between
compartments.
A summary of membrane
functions in a plant cell.

© 2013 John Wiley & Sons, Inc. All rights reserved.

 An Overview of Membrane Functions
• Transporting solutes (4)
Membrane proteins facilitate the
movement of substances between
compartments.
• Responding to external signals (5)
Membrane receptors transduce
signals from outside the cell in
response to specific ligands.
• Intercellular interaction (6)
Membranes mediate recognition
and interaction between adjacent
cells.
• Energy transduction (7)
Membranes transduce
photosynthetic energy, convert
chemical energy to ATP, and store A summary of membrane
energy. functions in a plant cell.

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 A Brief History of Studies on Plasma
Membrane Structure

• The fluid-mosaic model

• S. Jonathan Singer & Garth Nicolson (UC-San Diego, 1972) –
proposed it , the central dogma of membrane biology for >3 decades
• Core lipid bilayer exists in a fluid state, capable of movement.
• Membrane proteins form a mosaic of particles penetrating the
lipids.
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The Chemical Composition of Membranes
• Membrane composition
– The lipid and protein components are
bound together by non-covalent
bonds.
– Membranes also contain
carbohydrates.
– Protein/lipid ratios vary among
membrane types, type of organism,
cell type.

Myelin sheath:
Galactocerebroside

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 Chemical structure of membrane lipids
• Membrane lipids are Polar P Glycerol
amphipathic with three
main types: Fatty acid
• Phosphoglycerides are chain
diacylglycerides with
small functional head
groups linked to the
glycerol backbone by The chemical structure
phosphate ester bonds. of membrane lipids
• Sphingolipids are
ceramides formed by
the attachment of
sphingosine to fatty
acids; glycolipids
• Cholesterol is a smaller
and less amphipathic
lipid that is only found in
animals.
 Cholesterol
• A sterol that makes up to 50%
of animal membrane lipids.
• The -OH group is oriented
toward membrane surface
• Carbon rings are flat and rigid;
interfere with movement of
phospholipid fatty acid tails
•It prevents packing of
phospholipid tails and lowers
requirement of unsaturated fatty
acids.
•It makes the cell membrane
firm enough without becoming
too liquid at body temperature.
Cholesterol molecules (green) oriented with
their small hydrophilic end facing the external
surface of the bilayer
 Liposomes: synthetic vesicles

• The Nature and Importance of the Lipid Bilayer

– Membrane lipid composition is characteristic of specific membranes.
– Lipids give membranes the ability to fuse, form networks, and
separate charge.
– Lipid bilayers assemble spontaneously in aqueous solutions as in
liposomes.
The Asymmetry of Membrane Lipids
– Outer leaflet: glycolipids
Human erythrocyte Plasma
(receptors); PC, sphingomyelin Membrane
– Inner leaflets: PE, PS(-), PI (-);
negative charge cytosolic face
– Provides different physico-
chemical properties appropriate
for different interactions
– Membrane lipids move easily
within a leaflet but only rarely
“flip-flop”

SM: sphingomyelin PE: phosphatidylethanolamine

PC: phosphatidylcholine PI: phosphatidylinositol
PS: phosphatidylserine Cl: cholesterol
 Two types of
linkages that join
sugars to a
polypeptide chain

Blood-group
antigens

• Membrane Carbohydrates (glycosylation)

– Membranes with oligosaccharides covalently linked to lipids and proteins on
the extracellular surface of the bilayer ( glycocalyx: carbohydrate coat); face
away from cytosol internal cellular membrane
– Glycoproteins have short, branched carbohydrates for interactions with other
cells and structures outside the cell. N-linked to asparagine or O-linked to
serine or threonine
– Glycolipids have larger carbohydrate chains that may be cell-to-cell recognition
sites; carbohydrates of the glycolipid of RBCs plasma membrane determine
the person’s blood type; presence of enzyme/s that attaches terminal sugar
 Noncovalent Bonds
Hydrophobic interaction
- nonpolar molecules
associate and minimize
their exposure to polar
molecules by forming
aggregates or micelles
- lack charged region that
can interact with poles of
water molecules & are thus
insoluble in water
- Hydrophobic, nonpolar R
groups congregate in
soluble protein interior
away from H2O Hydrophobic interactions reduce
exposure to hydrophilic molecules
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 Noncovalent Bonds
4. Van de Waals forces:
• attractions between nonpolar
molecules or hydrophobic groups are
due to transient dipole formation
(change in electron distribution)
• Biological molecules must be close
together & interacting portions have
complementary shapes that allow
close approach; many atoms of both
interactants can approach each other
closely
• For example interactions between
antibodies and viral antigens
Van der Waals forces operate at
optimum distances and are maximized
by complementary surfaces.

© 2013 John Wiley & Sons, Inc. All rights reserved.

 The chemical
structures of
amino acids

A. Polar charged - contain R groups that act as stronger organic acids, bases; can
form ionic bonds
1. Almost always fully charged (lysine, arginine, aspartic acid, glutamic acid) at
pH 7; side chains are relatively strong organic acids & bases
2. Can form ionic bonds due to charges; histones with arginine (+-charge) bind
to negatively charged phosphate groups of DNA
3. Histidine - usually only partially charged at pH 7; often important in enzyme
active sites due to its ability gain or lose a proton in physiologic
pH ranges
 The chemical
structures of
amino acids

B. Polar uncharged - R groups weakly acidic or basic; not fully charged at pH 7; can
form H bonds with other molecules like water since they have
atoms with a partial negative or positive charge
Asparagine & glutamine [amides of aspartic & glutamic acid], threonine, serine, tyrosine

© 2013 John Wiley & Sons, Inc. All rights reserved.

 The chemical
structures of
amino acids

C. Nonpolar - R groups hydrophobic; generally lack O & N; cannot interact with

water or form electrostatic bonds; vary primarily in size & shape;
allows them to pack tightly into protein core
1. Alanine, valine, leucine, isoleucine, tryptophan, phenylalanine, methionine
2. Associate with one another via hydrophobic & van der Waals interactions in protein core

© 2013 John Wiley & Sons, Inc. All rights reserved.

 The chemical
structures of
amino acids

D. The other three – glycine, proline, cysteine

1. Glycine (R = H) - small R group makes backbone flexible & able to move so it is
useful in protein hinges; small R group allows 2 backbones (of same or different protein)
to approach closely
2. Proline – R group forms ring with amino group (imino acid); hydrophobic amino
acid that does not readily fit into orderly secondary structure (a-helix)
3. Cysteine – R group has reactive —SH; forms disulfide (—S—S—) bridge with other
cysteines often at some distance away in polypeptide backbone

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 The Structure and Functions of Membrane
Proteins
• Membrane proteins attach to the bilayer
asymmetrically, giving the membrane a distinct
“sidedness”
• Membrane proteins can be grouped into three
distinct classes:
1. Integral proteins - penetrate and pass
through lipid bilayer; make up 20 -30% of
all encoded proteins
• Are amphipathic, with hydrophobic
domains anchoring them in the bilayer
fatty acids and hydrophilic regions
forming functional domains outside of Integral proteins
the bilayer; solubilize by detergent
• Channel proteins have hydrophilic
cores that form aqueous channels in
the membrane-spanning region.
Functions of integral membrane proteins:
A. As receptors that bind specific
substances at the membrane surface
B. As channels or transporters involved
in the movement of ions & solutes across
the membrane
C. As agents that transfer electrons
during the processes of photosynthesis &
respiration

– Transmembrane domain:
Hydrophobic and Van der Waals
interactions Integral proteins

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 The Structure and Functions of
Membrane Proteins
2. Peripheral proteins
- attached to the membrane by weak
bonds to hydrophilic head groups of
lipids or to hydrophilic portions of
integral proteins protruding from
bilayer
- easily solubilized with aqueous salt
solution and extreme pH
– located entirely outside of bilayer on
either the extracellular or cytoplasmic
Peripheral proteins
side; associated with membrane
surface by non-covalent bonds ( ionic,
protein –protein interaction).
© 2013 John Wiley & Sons, Inc. All rights reserved.
2. Peripheral proteins Functions
– give mechanical support to
membrane & as an anchor for integral
proteins
– Other peripheral proteins on internal
membrane surface function as
enzymes, specialized coats or factors
that transmit transmembrane signals

Peripheral proteins
 The Structure and Functions of
Membrane Proteins
3. Lipid-anchored membrane proteins
are distinguished both by the types
of lipid anchor and their orientation.
– Glycophosphatidylinositol (GPI)-
linked proteins found on the
outer leaflet can be released by
inositol-specific phospholipases.
– Some inner-leaflet proteins are
anchored to membrane lipids by
long hydrocarbon chains.
Lipid-anchored proteins

© 2013 John Wiley & Sons, Inc. All rights reserved.

 Ectoplasmic
vs
protoplasmic

• Distribution of Integral Proteins: Freeze-

Fracture Analysis
– Freeze-fracture technique divides the
phospholipid leaflets of the membrane.
– Integral membrane proteins appear as
bumps and pits using the electron
microscope.
– The heterogeneity of protein distribution AB: carb group for glycophorin
is shown.

© 2013 John Wiley & Sons, Inc. All rights reserved.

 Solubilization of membrane
proteins with detergents

• Studying the Structure and Properties of Integral Membrane Proteins

– Determining membrane sidedness: The orientation of integral proteins
can be determined using non-penetrating agents that label the proteins.
– SDS (ionic)-denatures proteins; sodium dodecyl sulphate
– Triton X-100 (non-ionic)- does not alter protein tertiary structure

© 2013 John Wiley & Sons, Inc. All rights reserved.

 Glycophorin A, an integral protein
with a single transmembrane domain
with a Gly-X-X-X-Gly sequence

• Studying the Structure and Properties of Integral Membrane Proteins

– Identifying transmembrane domains: A string of 20-30 hydrophobic amino
acids make up α helix glycophorin monomer , membrane-spanning domain.
– Glycophorin A in erythrocytes: 2 identical helices of dimer; homodimers
 Erythrocyte plasma membrane model
viewed from the internal surface

• Integral Proteins of the Erythrocyte Membrane

– Band 3 is composed of two homodimers of a glycoprotein that
exchanges Cl– and HCO3– across the red cell membrane.
– Glycophorin A is a dimer with 16 oligosaccharide chains bearing negative
charges on sialic acid that may prevent red cells from clumping; used as
receptors in the erythrocytes for protozoans that cause malaria
• The Erythrocyte Membrane Skeleton
– The major component of the internal membrane skeleton is spectrin.
– Spectrin (heterodimer) attached to the membrane surface by noncovalent
bonds to ankyrin
– Spectrin is linked to other cytoplasmic proteins, such as actin and
tropomyosin, which maintains the integrity of the membrane; elasticity and
pliability
– Ankyrin: links spectrin to the cytosolic face of band 3.
 Membrane Lipids and Membrane Fluidity
Structure depends on the temperature

Structure of the lipid bilayer depends on the temperature:

above and below the transition temperature.

• The Importance of Membrane Fluidity

– The fluidity of membranes is a compromise between structural rigidity and
complete fluidity.
– Membrane fluidity makes it possible for proteins to move in the membrane
and for membranes to assemble and grow.
© 2013 John Wiley & Sons, Inc. All rights reserved.
 Membrane Lipids and Membrane
Fluidity
• Membrane lipids exist in gel or liquid-crystal phases depending
on:
– temperature
– lipid composition
– saturation in the presence of cholesterol
• Liquid-crystal membranes predominate
• At warm temperatures (370C), lipid is relatively fluid, liquidlike
state; a 2 dimensional liquid crystal
1. Molecules retain a specified orientation as in crystal;
molecule long axes stay essentially parallel
2. Yet individual molecules can rotate around axis or move
laterally within bilayer plane

© 2013 John Wiley & Sons, Inc. All rights reserved.

 Membrane Lipids and Membrane
Fluidity

• At colder temperatures, lipid is converted to frozen crystalline

gel in which phospholipid fatty acid chain movement is greatly
restricted
• Unsaturated fatty acids lower the temperature at which
the liquid-crystal/gel phase transition occurs (transition
temperature) or before the bilayer gels
• The shorter the fatty acyl chains of a phospholipid, the
lower the melting temperature.

© 2013 John Wiley & Sons, Inc. All rights reserved.

 Membrane Lipids and Membrane
Fluidity
Cholesterol –interacts with membrane phospholipid fatty acid
chains & alters the way the fatty acids pack together
1. Low temp.: disrupts the close packing of fatty acyl chains,
prevents from freezing, maintains membrane fluidity
High temp.: interferes with their mobility, outer layer less
fluid and reduce permeability to small molecules
2. It tends to abolish sharp transition temperatures & creates
a condition of intermediate fluidity.
3. It tends to raise membrane durability & lower membrane
permeability .

© 2013 John Wiley & Sons, Inc. All rights reserved.

 Structure depends on the temperature
Maintaining Membrane Fluidity
– Organisms (other than birds and mammals) maintain membrane
fluidity as temperature changes by altering the composition of
membrane lipids.
– To be cold resistant:
1. Fatty acyl chain single bonds are desaturated forming double
bonds; catalyzed by desaturases
2. Chains are reshuffled between different phospholipids to produce
those with 2 unsaturated chains; this greatly lowers the bilayer's melting
temperature
a. Reshuffling done by phospholipases (split fatty acids from
glycerol backbone)
b. Acyltransferases transfer the fatty acid chains to a different
phospholipid
3. Cell also changes the types of phospholipids synthesized to those
containing more unsaturated fatty acids
 The Dynamic Nature of the Plasma
Membrane
• Lipid bilayer can exist in a relatively fluid
state.
• A phospholipid can move laterally within
the same leaflet with considerable ease.
• In contrast, it takes a phospholipid
molecule a matter of hours to days to
move across to the other leaflet (flip-flop).
• The hydrophilic head group of the lipid
must pass through the internal
hydrophobic sheet of the membrane,
which is thermodynamically unfavorable.
• The physical state of the lipid is an
important determinant of the mobility of The possible movements of
integral proteins. phospholipids in a membrane

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Cell fusion to reveal mobility of membrane proteins:
fusion of human and mouse cells

• The Diffusion of Membrane Proteins after Cell Fusion

– Cell fusion is a technique whereby two different types of cells, or cells
from two different species, can be fused to produce one cell with a
common cytoplasm and a single, continuous plasma membrane.
– Cell fusion be induced by certain viruses, or with polyethylene glycol.
– Labeled proteins have shown that membrane proteins can move
between fused cell.
© 2013 John Wiley & Sons, Inc. All rights reserved.
 Differentiated functions of the plasma
membrane of an epithelial cell.

• Membrane Domains and Cell

Polarity
– Differences in protein
distribution are evident in
cells of organized tissues.
– In epithelia, the proteins of
the apical membrane are
distinct from those of the
lateral and basal
membranes
– Highly differentiated sperm
have a head, midpiece, and
tail that is covered by a
continuous membrane.

© 2013 John Wiley & Sons, Inc. All rights reserved.

 The Movement of Substances Across Cell
Membranes

1. Simple diffusion through

lipid bilayer
2. Simple diffusion through
an aqueous, protein-lined
channel
3. Facilitated diffusion via a
protein transporter
4. Active transport via an
ATP- protein pump Four basic mechanisms by which solute
molecules move across membranes

© 2013 John Wiley & Sons, Inc. All rights reserved.

• The Energetics of Solute Movement

– Diffusion is the spontaneous

movement of material from a
region of high concentration to a
region of low concentration.
– The free-energy change during
diffusion of nonelectrolytes
depends on the concentration
gradient.
– The free-energy change during
diffusion of electrolytes depends
on the electrochemical gradient.
– Very small, uncharged (inorganic)
molecules (O2, CO2 NO, H2O)
penetrate very rapidly between Four basic mechanisms by which solute
adjacent phospholipids molecules move across membranes

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 The tonicity of a solution mainly depends on its concentration of
solutes relative to the concentration of solutes inside the cell.

The effects of differences

in the concentration of
solutes on opposite sides
of the plasma membrane

– Diffusion of water through a semipermeable membrane is

called osmosis.
– Water diffuses from areas of lower solute concentration to
areas of higher solute concentration.
– Cells swell in hypotonic solution, shrink in hypertonic solutions,
and remain unchanged in isotonic solutions ( 0.90% NaCl
isotonic to human cells) .
• The Diffusion of Water
through Membranes
– Plant cells develop turgor
in hypotonic solutions
because cell walls prevent
swelling.
– In hypertonic solutions the
plant cell undergoes
plasmolysis.
– Aquaporins are specialized
protein channels that
allow passive movement
of water.
The effects of osmosis on a plant cell
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• Most ion channels are gated, either open
or closed
• 3 Major categories of gated channels:
1. Voltage-gated channels-
conformational state depends on the
difference in ionic charge on the 2
sides of membrane. Ex. Voltage-gated
K+ channel
2. Ligand-gated channels –
conformational state depends on
binding of specific molecule (the
ligand), which is usually not the solute 3D structure of
that passes through the channel. Ex. the bacterial
KcsA channel
Acetylcholine as ligand associated
and K+ ion
with Na+ channel selectivity

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 3. Mechano-gated
channels – conformational
state depends on
mechanical forces (e.g.,
stretch tension) that are
applied to the membrane
cation channels are opened
by the movements of
stereocilia on the hair cells
of the inner ear in
response to sound or
motions of the head

© 2013 John Wiley & Sons, Inc. All rights reserved.

 The structure of a
eukaryotic, voltage-
gated K+ channel

• Eukaryotic Kv channels
– Contain six membrane-associated helices (S1-S6).
– Six helices can be grouped into two domains:
• Pore domain – permits the selective passage of K+ ions.
• Voltage-sensing domain – consists of helices S1-S4 that senses the
voltage across the plasma membrane.

© 2013 John Wiley & Sons, Inc. All rights reserved.

• Eukaryotic Kv channels
– Once opened, more than
10 million K+ ions can pass
through per second.
– After the channel is open
for a few milliseconds, the
movement of K+ ions is
“automatically” stopped by Conformational states of a
voltage-gated K+ ion channel
a process known as
inactivation.
– Can exist in three different
states: open, inactivated,
and closed.

© 2013 John Wiley & Sons, Inc. All rights reserved.

• The Glucose Transporter: An Example of Facilitated Diffusion
– The gradient for glucose entry into the cell is maintained by
phosphorylation of glucose in the cytoplasm to lower
concentration in the cytoplasm.
– Insulin stimulates glucose uptake by causing the insertion into
the cell membrane of cytoplasmic vesicles containing
preformed glucose transporters, found in muscle cells and
adipocytes © 2013 John Wiley & Sons, Inc. All rights reserved.
• Active Transport
– Maintains the gradients for potassium, sodium, calcium, and other ions
across the cell membrane.
– Energy from ATP hydrolysis or stored potenital energy from an ion
gradient
– Forms: 1.) Uniport- carrier protein transports a single solute at a time;
ex. H+-ATPase, Ca+ pump
2.) Cotransport- 2 solutes at the same time by a single carrier
protein
2.1. Symport- both solutes in the same direction; ex.
Na+/glucose symport; sucrose/H+ symport
2.2. Antiport- opposite direction; ex. Na+/K+ ATPase, H+/K+
ATPase

© 2013 John Wiley & Sons, Inc. All rights reserved.

• Coupling Active Transport to ATP Hydrolysis
– The Na+/K+ ATPase (sodium-potassium pump)requires K+ outside, Na+ inside, and
is inhibited by ouabain.
– The ratio of Na+:K+ pumped is 3:2.
– The ATPase is a P-type pump, in which phosphorylation causes changes in
conformation and ion affinity that allow transport against gradients.
– V-type pumps: no phosphorylation of membrane protein; vacuolar/vesicular
H+-pump
 Control of acid
secretion in the
stomach

• Other Ion Transport Systems

– Other P-type pumps include H+ and Ca2+ ATPases, and H+/K+-ATPases.
– Vacuolar (V-type) pumps use ATP, but are not phosphorylated during pumping.
– ATP-binding cassette (ABC) transporters have regulatory ATP-binding sites.

© 2013 John Wiley & Sons, Inc. All rights reserved.

 Control of acid
secretion in the
stomach

1. At rest, found in cytoplasmic membranes of stomach lining parietal

cells & are nonfunctional
2. With food, hormonal message (gastrin) transmitted to parietal cells
that causes pump-containing membranes to move to apical surface
3. They fuse with apical surface membrane & secrete acid (aids digestion
but can lead to heartburn)
4. New acid-blocking medications (Zantac, Pepcid, Tagamet) do not
inhibit H+/K+-ATPase directly; they block parietal cell receptors & stop hormone
activation of cells & thus halt H+/K+-ATPase
5. Another drug, Prilosec, prevents heartburn by inhibiting stomach's
H+/K+-ATPase © 2013 John Wiley & Sons, Inc. All rights reserved.
• Co-transport: Coupling Active
Transport to Existing Ion
Gradients
• Gradients created by active
ion pumping store energy
that can be coupled to other
transport processes.
• Secondary transport: the use of
energy stored in an ionic gradient
• Na+/glucose symport:
• Na+ ion tendency to diffuse
back across apical membrane
is tapped by epithelial cells to
drive glucose molecule
cotransport into cell against
their concentration gradient
(2° active transport)
• Plant cells: sucrose, amino Secondary transporter: the Na+ gradient helps to
acid, nitrate driven by H+ transport glucose by a Na+/glucose co-transporter
ions
Secondary Transport: Antiport

© 2013 John Wiley & Sons, Inc. All rights reserved.

 Membrane Potentials and Nerve Impulses

• Electric/voltage potential differences

exist when charges are separated by
plasma membrane; permeabilities of
ions
– Membrane potentials have been
measured in all types of cells.
– Neurons are specialized cells for
information transmission using
changes in membrane
potentials.
– Resting Membrane Potential:
negative membrane potential
• Na+ /K+ ATPase ; K+ leak
channels
 Action Potentials
(AP)
• Occur only when membrane potential at axon
hillock reaches threshold
• Three phases:
– Depolarization: Voltage-gated Na+ channels
open
– Repolarization: Voltage-gated K+ channels
open
– Hyperpolarization : K+ channels open
• Absolute refractory period
– During or immediately following an AP
– Excitable cell incapable of generating a new
AP no matter how strong the stimulus is
• Relative refractory period
– Immediately following absolute refractory pd
– More difficult to generate new AP
– New AP if exposed to suprathreshold
stimulus
 Membrane Potentials and Nerve Impulses

• The Action Potential (AP)

– When cells are stimulated, Na+
channels open, causing membrane
depolarization.
– When cells are stimulated, voltage-
gated Na+ channels open, triggering
the AP.
– Na+ channels are inactivated
immediately following an AP,
producing a short refractory period
when the membrane cannot be
stimulated.
– Excitable membranes exhibit all-or-
none behavior.

Formation of an action potential

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 Propagation of an
impulse results from
the local flow of
ions unidirectionally

• Propagation of Action Potentials as an Impulse

– APs produce local membrane currents depolarizing adjacent membrane
regions of the membrane that propagate as a nerve impulse.
– Speed Is of the Essence: Speed of neural impulse depends on axon
diameter and whether axon is myelinated.
• Resistance to current flow decreases as diameter increases.
• Myelin sheaths cause saltatory conduction.
© 2013 John Wiley & Sons, Inc. All rights reserved.
 Saltatory conduction:
Propagation of an
impulse by forming an
action potential only at
the nodes of Ranvier

• APs occur at nodes of Ranvier

• Electrotonic current spread through internodes ( up
to a distance of 2-3mm in most organisms
• Neurotransmission: Jumping
the Synaptic Cleft
– Presynaptic neurons
communicate with postsynaptic
neurons at a specialized junction,
called the synapse, across a gap
(synaptic cleft).
– Chemicals (neurotransmitters)
released from the presynaptic
cleft diffuse to receptors on the
postsynaptic cell.
– Bound transmitter can depolarize
(excite) or hyperpolarize (inhibit)
the postsynaptic cell.
– Transmitter action is terminated
by reuptake or enzymatic
breakdown.
The neuromuscular junction

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Signal Transmission at a Chemical Synapse

Ca2+ bind to synap-

totagmin on
membrane of
synaptic vesicles
to enable it to
Interact with the
SNARE complex
for membrane
fusion

Figure 4.16
• Neurotransmitter binding to ion channel receptors can
either stimulate or inhibit action potential:
• Excitatory: acetylcholine
• Inhibitory: acetylcholine on skeletal muscle blood
vessels or heart ; gamma-aminobutyric acid (GABA);
general anesthetics

The sequence of events during synaptic transmission with

acetylcholine as the neurotransmitter
© 2013 John Wiley & Sons, Inc. All rights reserved.
Acetylcholine

Figure 4.17
• Actions of Drugs on Synapses
– Interference with the destruction or reuptake of
neurotransmitters can have dramatic physiological and
behavioral effects.
– Examples include: antidepressants, marijuana, cocaine

The sequence of events during synaptic transmission with

acetylcholine as the neurotransmitter
© 2013 John Wiley & Sons, Inc. All rights reserved.