Molecular genetic analyses of a 376-kilodalton Golgi complex membrane protein (giantin)
نویسندگان
چکیده
منابع مشابه
Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa.
The Golgi complex consists of a series of stacked cisternae in most eukaryotes. Morphological studies indicate the existence of intercisternal cross-bridge structures that may mediate stacking, but their identity is unknown. We have identified a 400-kDa protein, giantin, that is localized to the Golgi complex because its staining in double immunofluorescence experiments was coincident with that...
متن کاملGiantin is the major Golgi autoantigen in human anti-Golgi complex sera
Anti-Golgi complex antibodies (AGAs) are primarily associated with systemic lupus erythematosus and Sjögren's syndrome. Here we report on the immunoreactivity of AGAs against five Golgi autoantigens (giantin, golgin-245, golgin-160, golgin-95/GM130, and golgin-97) and provide data from epitope mapping on the most common Golgi autoantigen, namely giantin. A total of 80 human sera containing AGAs...
متن کاملCASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin.
Large coiled-coil proteins are being found in increasing numbers on the membranes of the Golgi apparatus and have been proposed to function in tethering of transport vesicles and in the organization of the Golgi stack. Members of one class of Golgi coiled-coil protein, comprising giantin and golgin-84, are anchored to the bilayer by a single C-terminal transmembrane domain (TMD). In this articl...
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A protein which acts specifically to target vesicles within the Golgi complex, rather than to or from it, has recently been described. But does this open the way to understanding intra-Golgi membrane traffic?
متن کاملThe 64-kilodalton membrane protein of Bacillus subtilis is also present as a multiprotein complex on membrane-free ribosomes.
The 64-kDa membrane protein of Bacillus subtilis is evidently involved in the attachment of secreting ribosomes to membrane. On immunoprecipitation with antibody to this protein, the solubilized particulate fraction, with or without prior chemical cross-linking, yields a complex of four proteins (64, 60, 41, and 36 kDa). This "S complex" was found to be associated with membrane-free ribosomes r...
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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 1994
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.14.4.2564