PMID- 10209123
OWN - NLM
STAT- MEDLINE
DCOM- 19990511
LR  - 20181201
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 9
IP  - 7
DP  - 1999 Apr 8
TI  - A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil
      proteins.
PG  - 381-4
AB  - 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.
FAU - Barr, F A
AU  - Barr FA
AD  - IBLS, Division of Biochemistry and Molecular Biology, Davidson Building,
      University of Glasgow, Glasgow G12 8QQ, UK. f.barr@bio.gla.ac.uk
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Autoantigens)
RN  - 0 (Carrier Proteins)
RN  - 0 (GOLGA4 protein, human)
RN  - 0 (Golga4 protein, mouse)
RN  - 0 (Golgi Matrix Proteins)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Rab6 protein)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - EC 3.6.5.2 (rab GTP-Binding Proteins)
RN  - EC 3.6.5.2 (ras Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Autoantigens/chemistry/genetics/*metabolism
MH  - Binding Sites
MH  - Carrier Proteins/*metabolism
MH  - Golgi Apparatus/*metabolism
MH  - Golgi Matrix Proteins
MH  - Green Fluorescent Proteins
MH  - HeLa Cells
MH  - Humans
MH  - Luminescent Proteins/genetics/metabolism
MH  - *Membrane Proteins
MH  - Mice
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - *rab GTP-Binding Proteins
MH  - ras Proteins/*metabolism
EDAT- 1999/04/21 00:00
MHDA- 1999/04/21 00:01
CRDT- 1999/04/21 00:00
PHST- 1999/04/21 00:00 [pubmed]
PHST- 1999/04/21 00:01 [medline]
PHST- 1999/04/21 00:00 [entrez]
AID - S0960-9822(99)80167-5 [pii]
PST - ppublish
SO  - Curr Biol. 1999 Apr 8;9(7):381-4.