Vessicle Sorting and Trafficing
(Lodish et al., 2000, Section 17.8, 17.10)
Molecules are directed to specific target vessicles by modification
or aggregation of these molecules with specific transmembrane proteins
in the target vessicles.
-
Carbohydrates attached to lysososomal bound proteins are phosphorylated
(Fig. 17.39).
-
Phophorylated proteins are attached to membrane bound proteins which have
lysosomal targeting alpha domain (Fig.
17.40).
-
Regulated vessicles have specific secretory proteins that aggregates
and targets vessicles to be regulated (HyperCell movie).
-
Localization of transmembrane vessicles to apical or basal membranes is
controlled by the presence of the transmembrane proteins Rab and V-SNARE
(Fig. 17.43)
Pro-proteins are cleaved into active proteins late in the secretion
process (Fig. 17.42).
At least three types of coated vessicles transport proteins from organelle
to organelle (Fig. 17.50).
-
Clathrin
golgi to lysosomes and plasma membrane and endocytosis (Fig.
17.53).
-
Coatamer I (COPI) golgi to ER
(Fig. 17.58).
-
Coatamer II (COPII) ER to golgi
Adapter proteins bind between coat protein and the vessicle membrane.
Dynamin completes the pinching off of the clathrin coated vessicle
(Fig 17.54).
Depolymerization (by cytosolic Hsc 70) of the clathrin and coatamer
exposes transmembrane proteins (V-SNARE) that direct the vessicle to its
destination by binding to the specific T-SNARE protein on the target organelle.
The fusion protein SNAP25 causes the vessicle to fuse with the target membrane
(Fig. 17.59).
Activity
Quiz
References:
Lodish, H., Berk, A., Zipursky, S.L., Matsudaira, P., Baltimore, D.,
Darnell, J., 2000, Molecular Cell Biology, 4th Ed., W.H. Freeman and Company,
NY, New York. ISBN 0-7167-3136-3.