Function of the Mon1-Ccz1 complex on endosomes
| Autor(en): | Cabrera, M. Engelbrecht-Vandré, S. Ungermann, C. |
Stichwörter: | carrier protein, 80700-39-6; Carrier Proteins; Vesicular Transport Proteins; animal; binding site; Binding Sites; biological activity; carrier protein; Carrier Proteins; chemistry; endosome; Endosomes; guanine nucleotide exchange factor; guanosine triphosphatase activating protein; lipid composition; longin domain; Longin domains; membrane binding; metabolism; Mon1-Ccz1 complex; multiprotein complex; protein domain; protein folding; protein function; protein localization; protein Mon1 Ccz1 complex; protein subunit; Rab GEFs; Rab protein; Rab7/Ypt7; sequence analysis; TRAPP complex; unclassified drug; vesicular transport protein, Article; Vesicular Transport Proteins; yeast, Animals; Yeasts | Erscheinungsdatum: | 2014 | Herausgeber: | Landes Bioscience | Journal: | Small GTPases | Volumen: | 5 | Ausgabe: | 3 | Zusammenfassung: | Rabs exist in two forms: the inactive GDP-and the active GTP-bound form. GEF proteins mediate the exchange of GDP for GTP and thereby activate Rabs. Although GEFs share a common action, which involves the opening of the Rab nucleotide binding site, they do not contain a conserved catalytic domain. Longin domains have been either found in several GEFs (TRAPP, DENN) or predicted by sequence analyses (Mon1-Ccz1, BLOC-3). At least in TRAPP, they serve as a platform for interaction with a GTPase. We recently generated a model of the predicted longin domains of the Mon1-Ccz1 complex based upon the structure of the respective TRAPP subunits. This allowed us to identify activity-related important regions of the complex. Moreover, we analyzed the GEF activity of Mon1-Ccz1 in the presence of membranes and uncovered that certain acidic phospholipids support the recruitment of the GEF complex. In this commentary, we will discuss our findings in a broader context. © 2014 Taylor & Francis Group, LLC. |
ISSN: | 21541248 | DOI: | 10.4161/sgtp.29040 | Externe URL: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84922220913&doi=10.4161%2fsgtp.29040&partnerID=40&md5=91ab79649232fdebeb07046167137924 |
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