PMID- 10477754
OWN - NLM
STAT- MEDLINE
DCOM- 19991014
LR  - 20191023
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 146
IP  - 5
DP  - 1999 Sep 6
TI  - Gamma-synergin: an EH domain-containing protein that interacts with
      gamma-adaptin.
PG  - 993-1004
AB  - The AP-1 adaptor complex is associated with the TGN, where it links selected
      membrane proteins to the clathrin lattice, enabling these proteins to be
      concentrated in clathrin-coated vesicles. To identify other proteins that
      participate in the clathrin-coated vesicle cycle at the TGN, we have carried out 
      a yeast two- hybrid library screen using the gamma-adaptin subunit of the AP-1
      complex as bait. Two novel, ubiquitously expressed proteins were found: p34,
      which interacts with both gamma-adaptin and alpha-adaptin, and gamma-synergin, an
      alternatively spliced protein with an apparent molecular mass of approximately
      110-190 kD, which only interacts with gamma-adaptin. gamma-Synergin is associated
      with AP-1 both in the cytosol and on TGN membranes, and it is strongly enriched
      in clathrin-coated vesicles. It binds directly to the ear domain of gamma-adaptin
      and it contains an Eps15 homology (EH) domain, although the EH domain is not part
      of the gamma-adaptin binding site. In cells expressing alpha-adaptin with the
      gamma-adaptin ear, a construct that goes mainly to the plasma membrane, much of
      the gamma-synergin is also rerouted to the plasma membrane, indicating that it
      follows AP-1 onto membranes rather than leading it there. The presence of an EH
      domain suggests that gamma-synergin links the AP-1 complex to another protein or 
      proteins.
FAU - Page, L J
AU  - Page LJ
AD  - Department of Clinical Biochemistry and Cambridge Institute for Medical Research,
      University of Cambridge, Cambridge CB2 2XY, England.
FAU - Sowerby, P J
AU  - Sowerby PJ
FAU - Lui, W W
AU  - Lui WW
FAU - Robinson, M S
AU  - Robinson MS
LA  - eng
SI  - GENBANK/AF169548
SI  - GENBANK/AF169549
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Adaptor Protein Complex 1)
RN  - 0 (Adaptor Protein Complex alpha Subunits)
RN  - 0 (Adaptor Protein Complex gamma Subunits)
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Carrier Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Syng protein, rat)
RN  - 0 (msps protein, Drosophila)
SB  - IM
MH  - Adaptor Protein Complex 1
MH  - Adaptor Protein Complex alpha Subunits
MH  - Adaptor Protein Complex gamma Subunits
MH  - Adaptor Proteins, Vesicular Transport
MH  - Alternative Splicing/genetics
MH  - Animals
MH  - Binding Sites
MH  - Brain/metabolism
MH  - Carrier Proteins/*chemistry/genetics/*metabolism
MH  - Cell Line
MH  - Cell Membrane/metabolism
MH  - Cloning, Molecular
MH  - Cytosol/metabolism
MH  - Dogs
MH  - *Drosophila Proteins
MH  - Golgi Apparatus/metabolism
MH  - Intracellular Membranes/metabolism
MH  - Liver/metabolism
MH  - Membrane Proteins/chemistry/genetics/*metabolism
MH  - Mice
MH  - Microtubule-Associated Proteins/chemistry/*genetics/metabolism
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - RNA, Messenger/analysis/genetics
MH  - Rats
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Sequence Deletion
MH  - Yeasts/genetics
PMC - PMC2169493
EDAT- 1999/09/09 00:00
MHDA- 1999/09/09 00:01
CRDT- 1999/09/09 00:00
PHST- 1999/09/09 00:00 [pubmed]
PHST- 1999/09/09 00:01 [medline]
PHST- 1999/09/09 00:00 [entrez]
AID - 10.1083/jcb.146.5.993 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Sep 6;146(5):993-1004. doi: 10.1083/jcb.146.5.993.