Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Golgin-84 is a rab1 binding partner involved in Golgi structure.

http://www.ncbi.nlm.nih.gov/pubmed/12656988

Members of the golgin family of coiled-coil proteins have been implicated in the tethering of vesicles to Golgi membranes and cisternal membranes to each other. Many also bind to rab GTPases. Golgin-84 is a membrane-anchored golgin that we now show binds preferentially to the GTP form of the rab1 GTPase. It is also present throughout the Golgi stack by immuno-EM. Antibodies to golgin-84 inhibit stacking of cisternal membranes in a cell-free assay for Golgi reassembly, whereas the cytoplasmic domain of golgin-84 stimulates stacking and increases the length of re-assembled stacks. Transient expression of golgin-84 in NRK cells helps prevent the disassembly of the Golgi apparatus normally triggered by treatment with brefeldin A. Together these data suggest that golgin-84 is involved in generating and maintaining the architecture of the Golgi apparatus.

Pubmed ID: 12656988 RIS Download

Mesh terms: Animals | Cells, Cultured | Cryoelectron Microscopy | Golgi Apparatus | Liver | Membrane Proteins | Microscopy, Immunoelectron | Mitosis | Molecular Sequence Data | Protein Binding | Rats | rab1 GTP-Binding Proteins

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIGMS NIH HHS, Id: R01 GM087364
  • Agency: NIGMS NIH HHS, Id: R01 GM087364-01
  • Agency: NIGMS NIH HHS, Id: R01 GM087364-02
  • Agency: NIGMS NIH HHS, Id: R01 GM087364-03

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.