Linked Life Data

10209123

Source:http://linkedlifedata.com/resource/pubmed/id/10209123

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1999-5-11
pubmed:abstractText
In recent years, a large number of coiled-coil proteins localised to the Golgi apparatus have been identified using antisera from human patients with a variety of autoimmune conditions [1]. Because of their common method of discovery and extensive regions of coiled-coil, they have been classified as a family of proteins, the golgins [1]. This family includes golgin-230/245/256, golgin-97, GM130/golgin-95, golgin-160/MEA-2/GCP170, giantin/macrogolgin and a related group of proteins - possibly splice variants - GCP372 and GCP364[2][3][4][5][6][7][8][9][10][11]. GM130 and giantin have been shown to function in the p115-mediated docking of vesicles with Golgi cisternae [12]. In this process, p115, another coiled-coil protein, is though to bind to giantin on vesicles and to GM130 on cisternae, thus acting as a tether holding the two together [12] [13]. Apart from giantin and GM130, none of the golgins has yet been assigned a function in the Golgi apparatus. In order to obtain clues as to the functions of the golgins, the targeting to the Golgi apparatus of two members of this family, golgin-230/245/256 and golgin-97, was investigated. Each of these proteins was shown to target to the Golgi apparatus through a carboxy-terminal domain containing a conserved tyrosine residue, which was critical for targeting. The domain preferentially bound to Rab6 on protein blots, and mutations that abolished Golgi targeting resulted in a loss of this interaction. Sequence analysis revealed that a family of coiled-coil proteins from mammals, worms and yeast contain this domain at their carboxyl termini. One of these proteins, yeast Imh1p, has previously been shown to have a tight genetic interaction with Rab6 [14]. On the basis of these data, it is proposed that this family of coiled-coil proteins functions in Rab6-regulated membrane-tethering events.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
381-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10209123-Amino Acid Sequence, pubmed-meshheading:10209123-Animals, pubmed-meshheading:10209123-Autoantigens, pubmed-meshheading:10209123-Binding Sites, pubmed-meshheading:10209123-Carrier Proteins, pubmed-meshheading:10209123-Golgi Apparatus, pubmed-meshheading:10209123-Green Fluorescent Proteins, pubmed-meshheading:10209123-HeLa Cells, pubmed-meshheading:10209123-Humans, pubmed-meshheading:10209123-Luminescent Proteins, pubmed-meshheading:10209123-Membrane Proteins, pubmed-meshheading:10209123-Mice, pubmed-meshheading:10209123-Molecular Sequence Data, pubmed-meshheading:10209123-Mutation, pubmed-meshheading:10209123-Protein Binding, pubmed-meshheading:10209123-Protein Structure, Tertiary, pubmed-meshheading:10209123-Recombinant Fusion Proteins, pubmed-meshheading:10209123-Sequence Homology, Amino Acid, pubmed-meshheading:10209123-rab GTP-Binding Proteins, pubmed-meshheading:10209123-ras Proteins
pubmed:year
1999
pubmed:articleTitle
A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins.
pubmed:affiliation
IBLS, Division of Biochemistry and Molecular Biology, Davidson Building, University of Glasgow, Glasgow G12 8QQ, UK. f.barr@bio.gla.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't