Abstract
We have recently identified an unusually large human protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins (EMBO J 15: 4262 – 4273, 1996). This protein, designated p532 based on its predicted molecular weight (EMBO J 15: 5738, 1996), contains multiple structural domains including two regions of seven internal repeats highly related to the cell cycle regulator RCC1, a guanine nucleotide exchange factor for the small GTP-binding protein Ran, seven β-repeat domains characteristic of the β subunit of heterotrimeric G proteins, three putative SH3 binding sites, a putative leucine-zipper and a carboxy-terminal HECT domain characteristic of E3 ubiquitin-protein ligases. Some of these domains are known to be involved in protein-protein interactions, suggesting the existence of p532-interacting proteins. To identify some of these proteins, we used the carboxy-terminal RCC1-like domain (RLD) of p532 in the yeast two-hybrid system. We report here the isolation of a clone that encodes the last 654 amino acid residues of the clathrin heavy chain. This interaction involves amino acid residues 1315 – 1557 of the clathrin heavy chain and the carboxy, but not the amino-terminal RLD of p532. p532 has been located in the cytosolic fraction as well as in the Golgi apparatus. The interaction between p532 and clathrin only occurs in the cytosol and is mediated by the formation of an ATP-dependent ternary complex with the heat shock protein, Hsp70. These observations suggest that p532 is involved in membrane transport processes.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 50 print issues and online access
$259.00 per year
only $5.18 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Rosa, J., Barbacid, M. A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70. Oncogene 15, 1–6 (1997). https://doi.org/10.1038/sj.onc.1201170
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/sj.onc.1201170
Keywords
This article is cited by
-
The HERC1 ubiquitin ligase regulates presynaptic membrane dynamics of central synapses
Scientific Reports (2020)
-
Functional and pathological relevance of HERC family proteins: a decade later
Cellular and Molecular Life Sciences (2016)
-
The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis
Nature Genetics (2001)