The Golgin Coiled-Coil Proteins of the Golgi Apparatus
Author(s) -
Sean Munro
Publication year - 2011
Publication title -
cold spring harbor perspectives in biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.011
H-Index - 173
ISSN - 1943-0264
DOI - 10.1101/cshperspect.a005256
Subject(s) - golgi apparatus , rab , biology , gtpase , microbiology and biotechnology , coiled coil , transmembrane protein , small gtpase , transport protein , endosome , function (biology) , endoplasmic reticulum , genetics , signal transduction , receptor , intracellular
A number of long coiled-coil proteins are present on the Golgi. Often referred to as "golgins," they are well conserved in evolution and at least five are likely to have been present in the last common ancestor of all eukaryotes. Individual golgins are found in different parts of the Golgi stack, and they are typically anchored to the membrane at their carboxyl termini by a transmembrane domain or by binding a small GTPase. They appear to have roles in membrane traffic and Golgi structure, but their precise function is in most cases unclear. Many have binding sites for Rab family GTPases along their length, and this has led to the suggestion that the golgins act collectively to form a tentacular matrix that surrounds the Golgi to capture Rab-coated membranes in the vicinity of the stack. Such a collective role might explain the lack of cell lethality seen following loss of some of the genes in human familial conditions or mouse models.
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