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Chapter 13 Summary

SCI231 Molecular Biology and Cell Biology

Cells continually adjust the composition of their plasma membrane
and internal compartments in rapid response to need. They use an
elaborate internal membrane system to add and remove cell-surface
Exocytosis: the secretory pathway delivers newly synthesized
proteins, carbs and lipids either to the plasma membrane or the
extracellular space.
Endocytosis: cells remove plasma membrane components and
deliver them to internal compartments (endosomes), from where
they can be recycled to the membrane or be delivered to lysosomes
for degradation. It is also used to capture nutrients.
Within a eukaryotic cell, transport vesicles continuously bud off from
one membrane and fuse with another, carrying membrane
components and soluble luminal molecules (cargo) from the lumen
and membrane of the donor to the lumen and membrane of the

target compartment.

This vesicular transport flows along highly

organized, directional routes that allows the
cell to secrete, eat, and remodel its plasma
membrane and organelles. The secretory
pathway leads outward from the ER towards
the Golgi apparatus and cell surface, with a
side route leading to lysosomes. The
endocytic pathway leads inward from the
plasma membrane.
In each case, retrieval pathways balance the
flow of membrane between compartments
in the opposite direction, bringing
membrane and selected proteins back to
the compartment of origin.
In the figure below and besides, the green

arrows are endocytic, the red are secretory, and blue are retrieval
Each transport vesicle that buds from a compartment must be
selective, taking up only the appropriate molecules and fusing only
with the target membrane.
The character of a compartment is defined by the composition of
the enclosing membrane: molecular markers displayed on the

cytosolic surface of the membrane serve as guidance cues for

incoming traffic to ensure that transport vesicles fuse only with the
correct compartment.
Most transport vesicles form from specialized, coated regions of
membrane. They bud off as coated vesicles, which have a
distinctive cage of proteins covering their cytosolic surface. Before
the vesicles fuse with a target membrane, they discard their coat, so
the membranes can interact directly and fuse.
The coat performs 2 main functions:
1. An inner coat concentrates specific membrane proteins in a
specialized patch, which then gives rise to the vesicle
membrane. In this way, the inner layer selects the appropriate
membrane molecules for transport.
2. An outer coat layer assembles into a curved, basketlike lattice
that deforms the membrane patch and thereby shapes the
There are 3 well-characterized types of coated vesicles,
distinguished by their major coat proteins. Each type is used for
different transport steps.
1. Clathrin-coated mediate transport from the Golgi apparatus
and from the plasma membrane.
2. COPI-coated Mediate transport from the ER and the Golgi
cisternae. They bud from the Golgi compartments.
3. COPII-coated Mediate transport from the ER and the Golgi
cisternae. They bud from the ER.
The major protein component of clathrin-coated vesicles is clathrin,
which forms the outer layer of the coat. Each clathrin subunit
consists of three large and three small polypeptide chains that
together form a 3-legged structure (triskelion). Clathrin triskelions
assemble into a basketlike framework of hexagons and pentagons to
form coated pits (buds) on the cytosolic surface of membranes.

(C) shows the heavy chains, and (D) shows the light chains. The
light chains link to the actin cytoskeleton, which helps generate
force for membrane budding and vesicle movement, and their
phosphorylation regulates clathrin coat assembly. The interwoven
legs of the clathrin triskelions form an outer shell from which the Nterminal domains of the triskelions protrude inward. These domains
bind to the adaptor proteins.
Adaptor proteins form a discrete inner layer of the coat,
positioned between the clathrin cage and the membrane. They bind
the clathrin coat to the membrane and trap various transmembrane
proteins, including receptors that capture soluble cargo molecules
inside the vesicle cargo receptors. In this way, the adaptor
proteins select a specific set of transmembrane proteins, together
with the soluble proteins that interact with them, and package them

into each newly formed clathrin-coated transport vesicle.

The above image shows the assembly and disassembly of a clathrin
coat. The assembly of the coat introduces curvature into the
membrane, which leads in turn to the formation of a coated bud (or
pit if its in the plasma membrane). The adaptor proteins bind both
clathrin triskelions and membrane-bound cargo receptors. Other
membrane-bending and fission proteins are recruited to the neck of
the budding vesicle, where sharp membrane curvature is
introduced. The coat is rapidly lost shortly after the vesicle buds off.
There are several types of adaptor proteins. The best characterized
have 4 different protein subunits; others are single-chain proteins.
Each type is specific for a different set of cargo receptors. Clathrincoated vesicles budding from different membranes use different
adaptor proteins and thus package different receptors and cargo

The assembly of adaptor proteins on the membrane is tightly

controlled, in part by the cooperative interaction of the adaptor
proteins with other components of the coat. The proteins act as
coincidence detectors that only assemble at the right time and
place, as several requirements must be met simultaneously to
stably bind them.
This figure shows lipid-induced
conformation switching of AP2, an
adaptor protein. Upon interaction
with the phosphoinositide
PI(4,5)P2 in the cytosolic leaflet of
the plasma membrane, AP2
rearranges so that binding sites
for cargo receptors become
exposed. Each AP2 complex binds
4 PI(4,5)P2 molecules. In the open
AP2 complex, two subunits bind
the cytosolic tails of cargo
receptors that display the
appropriate endocytosis signals.
These signals consist of short
amino acid sequence motifs.
When AP2 binds tightly to the
membrane, it induced curvature, which favors the binding of
additional AP2 complexes.