PMID- 10209125
OWN - NLM
STAT- MEDLINE
DCOM- 19990511
LR  - 20190728
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 9
IP  - 7
DP  - 1999 Apr 8
TI  - A novel Golgi-localisation domain shared by a class of coiled-coil peripheral
      membrane proteins.
PG  - 385-8
AB  - The mechanism by which peripheral membrane proteins are targeted to the
      cytoplasmic face of the Golgi apparatus is poorly understood. Previously, we have
      identified a carboxy-terminal domain of the trans-Golgi-network (TGN) protein
      p230 that is responsible for Golgi localisation [1]. Here, we report the
      identification of a similar Golgi-localisation domain (GLD, also termed the
      'GRIP' domain - see the paper by Munro and Nichols elsewhere in this issue) in a 
      family of putative peripheral membrane proteins from lower and higher eucaryotes.
      The majority of family members have a domain structure similar to that of p230,
      with extensive coiled-coil regions (>80%) and the potential GLD located in a
      non-coiled-coil domain at the carboxyl terminus. Previously reported proteins in 
      this family include human golgin-97 and Saccharomyces cerevisiae Imh1p. By
      constructing chimeric cDNAs encoding carboxy-terminal regions of these family
      members fused to green fluorescent protein (GFP), we have directly demonstrated
      that the GLD of p230, golgin-97, the newly identified human protein GCC1p and
      yeast Imh1p functions as a Golgi-targeting domain in transfected mammalian cells.
      Site-directed mutagenesis of the GLDs identified two conserved aromatic residues 
      that are critical for the function of this targeting domain. Endogenous p230 was 
      displaced from the Golgi membranes in transfected cells expressing high levels of
      GFP fused to the GLD of either p230 or golgin-97, indicating that different GLDs 
      interact with similar membrane determinants. Thus, we have identified a family of
      coiled-coil proteins that share a domain shown to be sufficient for the
      localisation of peripheral membrane proteins to the Golgi apparatus.
FAU - Kjer-Nielsen, L
AU  - Kjer-Nielsen L
AD  - Department of Pathology and Immunology, Monash University Medical School,
      Melbourne, Victoria, Australia 3181.
FAU - Teasdale, R D
AU  - Teasdale RD
FAU - van Vliet, C
AU  - van Vliet C
FAU - Gleeson, P A
AU  - Gleeson PA
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 (GOLGA4 protein, human)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Autoantigens
MH  - Binding Sites/genetics
MH  - COS Cells
MH  - Fluorescent Antibody Technique
MH  - Golgi Apparatus/*metabolism
MH  - Green Fluorescent Proteins
MH  - Humans
MH  - Luminescent Proteins/genetics/metabolism
MH  - Membrane Proteins/chemistry/*metabolism
MH  - Microscopy, Confocal
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
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)80168-7 [pii]
AID - 10.1016/s0960-9822(99)80168-7 [doi]
PST - ppublish
SO  - Curr Biol. 1999 Apr 8;9(7):385-8. doi: 10.1016/s0960-9822(99)80168-7.