PMID- 10512869
OWN - NLM
STAT- MEDLINE
DCOM- 19991202
LR  - 20181201
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 10
IP  - 10
DP  - 1999 Oct
TI  - High-copy suppressor analysis reveals a physical interaction between Sec34p and
      Sec35p, a protein implicated in vesicle docking.
PG  - 3317-29
AB  - A temperature-sensitive mutant, sec34-2, is defective in the late stages of
      endoplasmic reticulum (ER)-to-Golgi transport. A high-copy suppressor screen that
      uses the sec34-2 mutant has resulted in the identification of the SEC34
      structural gene and a novel gene called GRP1. GRP1 encodes a previously
      unidentified hydrophilic yeast protein related to the mammalian Golgi protein
      golgin-160. Although GRP1 is not essential for growth, the grp1Delta mutation
      displays synthetic lethal interactions with several mutations that result in ER
      accumulation and a block in the late stages of ER-to-Golgi transport, but not
      with those that block the budding of vesicles from the ER. Our findings suggest
      that Grp1p may facilitate membrane traffic indirectly, possibly by maintaining
      Golgi function. In an effort to identify genes whose products physically interact
      with Sec34p, we also tested the ability of overexpressed SEC34 to suppress known 
      secretory mutations that block vesicular traffic between the ER and the Golgi.
      This screen revealed that SEC34 specifically suppresses sec35-1. SEC34 encodes a 
      hydrophilic protein of approximately 100 kDa. Like Sec35p, which has been
      implicated in the tethering of ER-derived vesicles to the Golgi, Sec34p is
      predominantly soluble. Sec34p and Sec35p stably associate with each other to form
      a multiprotein complex of approximately 480 kDa. These data indicate that Sec34p 
      acts in conjunction with Sec35p to mediate a common step in vesicular traffic.
FAU - Kim, D W
AU  - Kim DW
AD  - Howard Hughes Medical Institute and the Department of Cell Biology, Yale
      University School of Medicine, New Haven, Connecticut 06510, USA.
FAU - Sacher, M
AU  - Sacher M
FAU - Scarpa, A
AU  - Scarpa A
FAU - Quinn, A M
AU  - Quinn AM
FAU - Ferro-Novick, S
AU  - Ferro-Novick S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Autoantigens)
RN  - 0 (COG2 protein, S cerevisiae)
RN  - 0 (Carrier Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (GOLGA3 protein, human)
RN  - 0 (Golgi Matrix Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (RUD3 protein, S cerevisiae)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Vesicular Transport Proteins)
RN  - 0 (phosphatidylinositol receptors)
RN  - EC 3.4.- (Carboxypeptidases)
RN  - EC 3.4.16.5 (Cathepsin A)
SB  - IM
MH  - Amino Acid Sequence
MH  - Autoantigens/chemistry
MH  - Carboxypeptidases/metabolism
MH  - *Carrier Proteins
MH  - Cathepsin A
MH  - Cloning, Molecular
MH  - Endoplasmic Reticulum/genetics/metabolism
MH  - Fungal Proteins/chemistry/*genetics
MH  - Golgi Apparatus/genetics/metabolism
MH  - Golgi Matrix Proteins
MH  - Membrane Proteins/*genetics
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Receptors, Cytoplasmic and Nuclear
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Alignment
MH  - Suppression, Genetic
MH  - Vesicular Transport Proteins
MH  - Yeasts/*genetics
PMC - PMC25597
EDAT- 1999/10/08 00:00
MHDA- 1999/10/08 00:01
CRDT- 1999/10/08 00:00
PHST- 1999/10/08 00:00 [pubmed]
PHST- 1999/10/08 00:01 [medline]
PHST- 1999/10/08 00:00 [entrez]
AID - 10.1091/mbc.10.10.3317 [doi]
PST - ppublish
SO  - Mol Biol Cell. 1999 Oct;10(10):3317-29. doi: 10.1091/mbc.10.10.3317.