Protein transport to the vacuole and receptor-mediated endocytosis by clathrin heavy chain-deficient yeast

doi:10.1083/jcb.106.5.1453

This Article

	Full Text (PDF, 2160K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Payne, G. S.
	Articles by Schekman, R.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Payne, G. S.
	Articles by Schekman, R.


Social Bookmarking

	What's this?

ARTICLES

Protein transport to the vacuole and receptor-mediated endocytosis by clathrin heavy chain-deficient yeast

GS Payne, D Baker, E van Tuinen and R Schekman
Department of Biochemistry, University of California, Berkeley 94720.

Clathrin heavy chain-deficient mutants (chcl) of Saccharomyces cerevisiae are viable but exhibit compromised growth rates. To investigate the role of clathrin in intercompartmental protein transport, two pathways have been monitored in chcl cells: transport of newly synthesized vacuolar proteins to the vacuole and receptor- mediated uptake of mating pheromone. Newly synthesized precursors of the vacuolar protease carboxypeptidase Y (CPY) were converted to mature CPY with similar kinetics in mutant and wild-type cells. chcl cells did not aberrantly secrete CPY and immunolocalization techniques revealed most of the CPY in chcl cells within morphologically identifiable vacuolar structures. Receptor-mediated internalization of the mating pheromone alpha-factor occurred in chcl cells at 36-50% wild-type levels. The mutant cells were fully competent to respond to pheromone- induced cell-cycle arrest. These results argue that in yeast, clathrin may not play an essential role either in vacuolar protein sorting and delivery or in receptor-mediated endocytosis of alpha-factor. Alternative mechanisms ordinarily may execute these pathways, or be activated in clathrin-deficient cells.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

Fei, W., Alfaro, G., Muthusamy, B.-P., Klaassen, Z., Graham, T. R., Yang, H., Beh, C. T. (2008). Genome-Wide Analysis of Sterol-Lipid Storage and Trafficking in Saccharomyces cerevisiae. Eukaryot Cell 7: 401-414 [Abstract] [Full Text]
Aronova, S., Wedaman, K., Anderson, S., Yates, J. III, Powers, T. (2007). Probing the Membrane Environment of the TOR Kinases Reveals Functional Interactions between TORC1, Actin, and Membrane Trafficking in Saccharomyces cerevisiae. Mol. Biol. Cell 18: 2779-2794 [Abstract] [Full Text]
Ren, G., Vajjhala, P., Lee, J. S., Winsor, B., Munn, A. L. (2006). The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy. Microbiol. Mol. Biol. Rev. 70: 37-120 [Abstract] [Full Text]
Baggett, J. J., D'Aquino, K. E., Wendland, B. (2003). The Sla2p Talin Domain Plays a Role in Endocytosis in Saccharomyces cerevisiae. Genetics 165: 1661-1674 [Abstract] [Full Text]
Deloche, O., Schekman, R. W. (2002). Vps10p Cycles between the TGN and the Late Endosome via the Plasma Membrane in Clathrin Mutants. Mol. Biol. Cell 13: 4296-4307 [Abstract] [Full Text]
Henry, K. R., D'Hondt, K., Chang, J., Newpher, T., Huang, K., Hudson, R. T., Riezman, H., Lemmon, S. K. (2002). Scd5p and Clathrin Function Are Important for Cortical Actin Organization, Endocytosis, and Localization of Sla2p in Yeast. Mol. Biol. Cell 13: 2607-2625 [Abstract] [Full Text]
Howard, J. P., Hutton, J. L., Olson, J. M., Payne, G. S. (2002). Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. JCB 157: 315-326 [Abstract] [Full Text]
Feng, Y., Davis, N. G. (2000). Akr1p and the Type I Casein Kinases Act prior to the Ubiquitination Step of Yeast Endocytosis: Akr1p Is Required for Kinase Localization to the Plasma Membrane. Mol. Cell. Biol. 20: 5350-5359 [Abstract] [Full Text]
Hirst, J., Lui, W. W.Y., Bright, N. A., Totty, N., Seaman, M. N.J., Robinson, M. S. (2000). A Family of Proteins with {gamma}-Adaptin and VHS Domains that Facilitate Trafficking between the Trans-Golgi Network and the Vacuole/Lysosome. JCB 149: 67-80 [Abstract] [Full Text]
Roth, A. F., Davis, N. G. (2000). Ubiquitination of the PEST-like Endocytosis Signal of the Yeast a-Factor Receptor. J. Biol. Chem. 275: 8143-8153 [Abstract] [Full Text]
Bensen, E. S., Costaguta, G., Payne, G. S. (2000). Synthetic Genetic Interactions With Temperature-Sensitive Clathrin in Saccharomyces cerevisiae: Roles for Synaptojanin-Like Inp53p and Dynamin-Related Vps1p in Clathrin-Dependent Protein Sorting at the trans-Golgi Network. Genetics 154: 83-97 [Abstract] [Full Text]
Chen, C.-Y., Ingram, M. F., Rosal, P. H., Graham, T. R. (1999). Role for Drs2p, a P-Type ATPase and Potential Aminophospholipid Translocase, in Yeast Late Golgi Function. JCB 147: 1223-1236 [Abstract] [Full Text]
Chen, C.-Y., Graham, T. R. (1998). An arf1{Delta} Synthetic Lethal Screen Identifies a New Clathrin Heavy Chain Conditional Allele That Perturbs Vacuolar Protein Transport in Saccharomyces cerevisiae. Genetics 150: 577-589 [Abstract] [Full Text]
Roth, A. F., Sullivan, D. M., Davis, N. G. (1998). A Large PEST-like Sequence Directs the Ubiquitination, Endocytosis, and Vacuolar Degradation of the Yeast a-Factor Receptor. JCB 142: 949-961 [Abstract] [Full Text]
Huang, K., Gullberg, L, Nelson, K., Stefan, C., Blumer, K, Lemmon, S. (1997). Novel functions of clathrin light chains: clathrin heavy chain trimerization is defective in light chain-deficient yeast. J. Cell Sci. 110: 899-910 [Abstract]
Chu, D. S., Pishvaee, B., Payne, G. S. (1996). The Light Chain Subunit Is Required for Clathrin Function in Saccharomyces cerevisiae. J. Biol. Chem. 271: 33123-33130 [Abstract] [Full Text]
Singer-Kruger, B, Stenmark, H, Zerial, M (1995). Yeast Ypt51p and mammalian Rab5: counterparts with similar function in the early endocytic pathway. J. Cell Sci. 108: 3509-3521 [Abstract]
Rad, M., Phan, H., Kirchrath, L, Tan, P., Kirchhausen, T, Hollenberg, C., Payne, G. (1995). Saccharomyces cerevisiae Apl2p, a homologue of the mammalian clathrin AP beta subunit, plays a role in clathrin-dependent Golgi functions. J. Cell Sci. 108: 1605-1615 [Abstract]
Payne, G., Schekman, R (1989). Clathrin: a role in the intracellular retention of a Golgi membrane protein. Science 245: 1358-1365 [Abstract]
Brodsky, F. (1988). Living with clathrin: its role in intracellular membrane traffic. Science 242: 1396-1402 [Abstract]
Howard, J. P., Hutton, J. L., Olson, J. M., Payne, G. S. (2002). Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. JCB 157: 315-326 [Abstract] [Full Text]