Oligomerization and dissociation of AP-1 adaptors are regulated by cargo signals and by ArfGAP1-induced GTP hydrolysis.
| Title: | Oligomerization and dissociation of AP-1 adaptors are regulated by cargo signals and by ArfGAP1-induced GTP hydrolysis. |
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| Authors: | Meyer DM; Biozentrum, University of Basel, CH-4056 Basel, Switzerland.; Crottet P; Maco B; Degtyar E; Cassel D; Spiess M |
| Source: | Molecular biology of the cell [Mol Biol Cell] 2005 Oct; Vol. 16 (10), pp. 4745-54. Date of Electronic Publication: 2005 Aug 10. |
| Publication Type: | Journal Article; Research Support, Non-U.S. Gov't |
| Language: | English |
| Journal Info: | Publisher: American Society for Cell Biology Country of Publication: United States NLM ID: 9201390 Publication Model: Print-Electronic Cited Medium: Print ISSN: 1059-1524 (Print) Linking ISSN: 10591524 NLM ISO Abbreviation: Mol Biol Cell Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Bethesda, MD : American Society for Cell Biology, c1992- |
| MeSH Terms: | GTPase-Activating Proteins/*metabolism ; Guanosine Triphosphate/*metabolism ; Protein Sorting Signals/*physiology ; Transcription Factor AP-1/*metabolism; Adaptor Protein Complex 2/metabolism ; Cell Membrane/metabolism ; Clathrin/metabolism ; Clathrin-Coated Vesicles/metabolism ; Cytosol/metabolism ; Liposomes/metabolism ; Animals ; COS Cells ; Cattle ; Chlorocebus aethiops ; Hydrolysis ; In Vitro Techniques ; Molecular Weight |
| Abstract: | The mechanism of AP-1/clathrin coat formation was analyzed using purified adaptor proteins and synthetic liposomes presenting tyrosine sorting signals. AP-1 adaptors recruited in the presence of Arf1.GTP and sorting signals were found to oligomerize to high-molecular-weight complexes even in the absence of clathrin. The appendage domains of the AP-1 adaptins were not required for oligomerization. On GTP hydrolysis induced by the GTPase-activating protein ArfGAP1, the complexes were disassembled and AP-1 dissociated from the membrane. AP-1 stimulated ArfGAP1 activity, suggesting a role of AP-1 in the regulation of the Arf1 "GTPase timer." In the presence of cytosol, AP-1 could be recruited to liposomes without sorting signals, consistent with the existence of docking factors in the cytosol. Under these conditions, however, AP-1 remained monomeric, and recruitment in the presence of GTP was short-lived. Sorting signals allowed stable recruitment and oligomerization also in the presence of cytosol. These results suggest a mechanism whereby initial assembly of AP-1 with Arf1.GTP and ArfGAP1 on the membrane stimulates Arf1 GTPase activity, whereas interaction with cargo induces oligomerization and reduces the rate of GTP hydrolysis, thus contributing to efficient cargo sorting. |
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| Substance Nomenclature: | 0 (Adaptor Protein Complex 2); 0 (Clathrin); 0 (GTPase-Activating Proteins); 0 (Liposomes); 0 (Protein Sorting Signals); 0 (Transcription Factor AP-1); 86-01-1 (Guanosine Triphosphate) |
| Entry Date(s): | Date Created: 20050812 Date Completed: 20060214 Latest Revision: 20191210 |
| Update Code: | 20260130 |
| PubMed Central ID: | PMC1237080 |
| DOI: | 10.1091/mbc.e05-06-0568 |
| PMID: | 16093346 |
| Database: | MEDLINE |
Journal Article; Research Support, Non-U.S. Gov't