The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery

Kucharczyk R, Hoffman-Sommer M, Piekarska I, Fischer von Mollard G, Rytka J (2009)
FEMS YEAST RESEARCH 9(4): 565-573.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Kucharczyk, Roza; Hoffman-Sommer, Marta; Piekarska, Iga; Fischer von Mollard, GabrieleUniBi ; Rytka, Joanna
Abstract / Bemerkung
The yeast protein Ccz1p is necessary for vacuolar protein trafficking and biogenesis. In a complex with Mon1p, it mediates fusion of transport intermediates with the vacuole membrane by activating the small GTPase Ypt7p. Additionally, genetic data suggest a role of Ccz1p in earlier transport steps, in the Golgi. In a search for further proteins interacting with Ccz1p, we identified the endosomal soluble N-ethylmaleimide-sensitive factor attachment protein receptor Pep12p as an interaction partner of Ccz1p. Combining the ccz1 Delta mutation with deletions of PEP12 or other genes encoding components of the endosomal fusion machinery, VPS21, VPS9 or VPS45, results in synthetic growth phenotypes. The genes MON1 and YPT7 also interact genetically with PEP12. These results suggest that the Ccz1p-Mon1p-Ypt7p complex is involved in fusion of transport vesicles to multiple target membranes in yeast cells.
Stichworte
vesicular transport; yeast; Ccz1p; late endosome
Erscheinungsjahr
2009
Zeitschriftentitel
FEMS YEAST RESEARCH
Band
9
Ausgabe
4
Seite(n)
565-573
ISSN
1567-1356
eISSN
1567-1364
Page URI
https://pub.uni-bielefeld.de/record/1633891

Zitieren

Kucharczyk R, Hoffman-Sommer M, Piekarska I, Fischer von Mollard G, Rytka J. The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery. FEMS YEAST RESEARCH. 2009;9(4):565-573.
Kucharczyk, R., Hoffman-Sommer, M., Piekarska, I., Fischer von Mollard, G., & Rytka, J. (2009). The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery. FEMS YEAST RESEARCH, 9(4), 565-573. https://doi.org/10.1111/j.1567-1364.2009.00515.x
Kucharczyk, Roza, Hoffman-Sommer, Marta, Piekarska, Iga, Fischer von Mollard, Gabriele, and Rytka, Joanna. 2009. “The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery”. FEMS YEAST RESEARCH 9 (4): 565-573.
Kucharczyk, R., Hoffman-Sommer, M., Piekarska, I., Fischer von Mollard, G., and Rytka, J. (2009). The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery. FEMS YEAST RESEARCH 9, 565-573.
Kucharczyk, R., et al., 2009. The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery. FEMS YEAST RESEARCH, 9(4), p 565-573.
R. Kucharczyk, et al., “The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery”, FEMS YEAST RESEARCH, vol. 9, 2009, pp. 565-573.
Kucharczyk, R., Hoffman-Sommer, M., Piekarska, I., Fischer von Mollard, G., Rytka, J.: The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery. FEMS YEAST RESEARCH. 9, 565-573 (2009).
Kucharczyk, Roza, Hoffman-Sommer, Marta, Piekarska, Iga, Fischer von Mollard, Gabriele, and Rytka, Joanna. “The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery”. FEMS YEAST RESEARCH 9.4 (2009): 565-573.

4 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Maturation of autophagosomes and endosomes: a key role for Rab7.
Hyttinen JM, Niittykoski M, Salminen A, Kaarniranta K., Biochim Biophys Acta 1833(3), 2013
PMID: 23220125
Tethering complexes in the endocytic pathway: CORVET and HOPS.
Solinger JA, Spang A., FEBS J 280(12), 2013
PMID: 23351085
Mon1a protein acts in trafficking through the secretory apparatus.
Bagley DC, Paradkar PN, Kaplan J, Ward DM., J Biol Chem 287(30), 2012
PMID: 22665492
Subunit organization and Rab interactions of Vps-C protein complexes that control endolysosomal membrane traffic.
Plemel RL, Lobingier BT, Brett CL, Angers CG, Nickerson DP, Paulsel A, Sprague D, Merz AJ., Mol Biol Cell 22(8), 2011
PMID: 21325627

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