SIGNAL-MEDIATED SORTING OF MEMBRANE PROTEINS BETWEEN THE ENDOPLASMIC RETICULUM AND THE GOLGI APPARATUS

Each organelle of the secretory pathway is required to selectively allow transit of newly synthesized secretory and plasma membrane proteins and also to maintain a unique set of resident proteins that define its structural and functional properties. In the case of the endoplasmic reticulum (ER), res...

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Bibliographic Details
Published in:Annual review of cell and developmental biology 1996-01, Vol.12 (1), p.27-54
Main Authors: Teasdale, Rohan D, Jackson, Michael R
Format: Article
Language:English
Subjects:
Animals
Biological Transport
Endoplasmic Reticulum - metabolism
Golgi Apparatus - metabolism
Humans
intracellular membranes
membrane proteins
Membrane Proteins - metabolism
protein targeting
retrograde transport
Sequence Analysis
Signal Transduction
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Summary:Each organelle of the secretory pathway is required to selectively allow transit of newly synthesized secretory and plasma membrane proteins and also to maintain a unique set of resident proteins that define its structural and functional properties. In the case of the endoplasmic reticulum (ER), residency is achieved in two ways: ( a ) prevention of residents from entering newly forming transport vesicles and ( b ) retrieval of those residents that escape. The latter mechanism is directed by discrete retrieval motifs: Soluble proteins have a H/KDEL sequence at their carboxy-terminus; membrane proteins have a dibasic motif, either di-lysine or di-arginine, located close to the terminus of their cytoplasmic domain. Recently it was found that di-lysine motifs bind the complex of cytosolic coat proteins, COP I, and that this interaction functions in the retrieval of proteins from the Golgi to the ER. Also discussed are the potential roles this interaction may have in vesicular trafficking.
ISSN:1081-0706
1530-8995
DOI:10.1146/annurev.cellbio.12.1.27