SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation

doi:10.1083/jcb.131.2.325

This Article

	Full Text (PDF, 2201K)
	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 Gimeno, R. E.
	Articles by Kaiser, C. A.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Gimeno, R. E.
	Articles by Kaiser, C. A.


Social Bookmarking

	What's this?

ARTICLES

SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation

RE Gimeno, P Espenshade and CA Kaiser
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.

SEC16 is required for transport vesicle budding from the ER in Saccharomyces cerevisiae, and encodes a large hydrophilic protein found on the ER membrane and as part of the coat of transport vesicles. In a screen to find functionally related genes, we isolated SED4 as a dosage- dependent suppressor of temperature-sensitive SEC16 mutations. Sed4p is an integral ER membrane protein whose cytosolic domain binds to the COOH-terminal domain of Sec16p as shown by two-hybrid assay and coprecipitation. The interaction between Sed4p and Sec16p probably occurs before budding is complete, because Sed4p is not found in budded vesicles. Deletion of SED4 decreases the rate of ER to Golgi transport, and exacerbates mutations defective in vesicle formation, but not those that affect later steps in the secretory pathway. Thus, Sed4p is important, but not necessary, for vesicle formation at the ER. Sec12p, a close homologue of Sed4p, also acts early in the assembly of transport vesicles. However, SEC12 performs a different function than SED4 since Sec12p does not bind Sec16p, and genetic tests show that SEC12 and SED4 are not functionally interchangeable. The importance of Sed4p for vesicle formation is underlined by the isolation of a phenotypically silent mutation, sar1-5, that produces a strong ER to Golgi transport defect when combined with sed4 mutations. Extensive genetic interactions between SAR1, SED4, and SEC16 show close functional links between these proteins and imply that they might function together as a multisubunit complex on the ER membrane.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Raychaudhuri, S., Prinz, W. A. (2008). Nonvesicular phospholipid transfer between peroxisomes and the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 105: 15785-15790 [Abstract] [Full Text]
Ivan, V., de Voer, G., Xanthakis, D., Spoorendonk, K. M., Kondylis, V., Rabouille, C. (2008). Drosophila Sec16 Mediates the Biogenesis of tER Sites Upstream of Sar1 through an Arginine-Rich Motif. Mol. Biol. Cell 19: 4352-4365 [Abstract] [Full Text]
Bhattacharyya, D., Glick, B. S. (2007). Two Mammalian Sec16 Homologues Have Nonredundant Functions in Endoplasmic Reticulum (ER) Export and Transitional ER Organization. Mol. Biol. Cell 18: 839-849 [Abstract] [Full Text]
Sato, K. (2004). COPII Coat Assembly and Selective Export from the Endoplasmic Reticulum. J Biochem 136: 755-760 [Abstract] [Full Text]
Supek, F., Madden, D. T., Hamamoto, S., Orci, L., Schekman, R. (2002). Sec16p potentiates the action of COPII proteins to bud transport vesicles. JCB 158: 1029-1038 [Abstract] [Full Text]
Taxis, C., Vogel, F., Wolf, D. H. (2002). ER-Golgi Traffic Is a Prerequisite for Efficient ER Degradation. Mol. Biol. Cell 13: 1806-1818 [Abstract] [Full Text]
Ram, R. J., Li, B., Kaiser, C. A. (2002). Identification of Sec36p, Sec37p, and Sec38p: Components of Yeast Complex That Contains Sec34p and Sec35p. Mol. Biol. Cell 13: 1484-1500 [Abstract] [Full Text]
Takai, Y., Sasaki, T., Matozaki, T. (2001). Small GTP-Binding Proteins. Physiol. Rev. 81: 153-208 [Abstract] [Full Text]
Hauri, H., Kappeler, F, Andersson, H, Appenzeller, C (2000). ERGIC-53 and traffic in the secretory pathway. J. Cell Sci. 113: 587-596 [Abstract]
Gilstring, C. F., Melin-Larsson, M., Ljungdahl, P. O. (1999). Shr3p Mediates Specific COPII Coatomer-Cargo Interactions Required for the Packaging of Amino Acid Permeases Into ER-derived Transport Vesicles. Mol. Biol. Cell 10: 3549-3565 [Abstract] [Full Text]
Levin, P. A., Kurtser, I. G., Grossman, A. D. (1999). Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 96: 9642-9647 [Abstract] [Full Text]
Roberg, K. J., Crotwell, M., Espenshade, P., Gimeno, R., Kaiser, C. A. (1999). LST1 Is a SEC24 Homologue Used for Selective Export of the Plasma Membrane ATPase from the Endoplasmic Reticulum. JCB 145: 659-672 [Abstract] [Full Text]
Chen, E. J., Frand, A. R., Chitouras, E., Kaiser, C. A. (1998). A Link between Secretion and Pre-mRNA Processing Defects in Saccharomyces cerevisiae and the Identification of a Novel Splicing Gene, RSE1. Mol. Cell. Biol. 18: 7139-7146 [Abstract] [Full Text]
Shaywitz, D. A., Espenshade, P. J., Gimeno, R. E., Kaiser, C. A. (1997). COPII Subunit Interactions in the Assembly of the Vesicle Coat. J. Biol. Chem. 272: 25413-25416 [Abstract] [Full Text]
Campbell, J.�L., Schekman, R. (1997). Selective packaging of cargo molecules into endoplasmic reticulum-derived�COPII�vesicles. Proc. Natl. Acad. Sci. USA 94: 837-842 [Abstract] [Full Text]