Abstract:
:Coatomer, the coat protein of coat protein complex (COP)I-vesicles, is a soluble protein complex made up of seven subunits, alpha-, beta-, beta'-, gamma-, delta-, epsilon-, and zeta-COP. Higher eukaryotes have two paralogous versions of the gamma- and zeta- subunits, termed gamma1- and gamma2-COP and zeta1- and zeta2-COP. Different combinations of these subunits are known to exist within coatomer complexes, and gamma1/zeta1-, gamma1/zeta2-, and gamma2/zeta1-COP represent the major coatomer populations in mammals. The role of COPI vesicles in the early secretory pathway is the subject of considerable debate. To help to resolve this discussion, we used quantitative immunoelectron microscopy and found that significant localization differences for COPI-isoforms do exist, with a preference for gamma1zeta1- and gamma1zeta2-coatomer in the early Golgi apparatus and gamma2zeta1-coatomer in the late Golgi apparatus. These differences suggest distinct functions for coatomer isoforms in a manner similar to clathrin/adaptor vesicles, where different adaptor proteins serve particular transport routes.
journal_name
Proc Natl Acad Sci U S Aauthors
Moelleken J,Malsam J,Betts MJ,Movafeghi A,Reckmann I,Meissner I,Hellwig A,Russell RB,Söllner T,Brügger B,Wieland FTdoi
10.1073/pnas.0611360104subject
Has Abstractpub_date
2007-03-13 00:00:00pages
4425-30issue
11eissn
0027-8424issn
1091-6490pii
0611360104journal_volume
104pub_type
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