HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 9, 6200-6206, March 2, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/9/6200    most recent M009191200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Takita, Y. Articles by Cunningham, K. W. Search for Related Content PubMed PubMed Citation Articles by Takita, Y. Articles by Cunningham, K. W. Social Bookmarking                      What's this?

Inhibition of the Ca²⁺-ATPase Pmc1p by the v-SNARE Protein Nyv1p^*

Yoko Takita, Laura Engstrom, Christian Ungermann, and Kyle W. Cunningham^§

From the Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218 and  Biochemie-Zentrum Heidelberg, Universität Heidelberg, D-69120 Heidelberg, Germany

Pmc1p, the Ca²⁺-ATPase of budding yeast related to plasma membrane Ca²⁺-ATPases of animals, is transcriptionally up-regulated in response to signaling by the calmodulin-calcineurin-Tcn1p/Crz1p signaling pathway. Little is known about post-translational regulation of Pmc1p. In a genetic screen for potential negative regulators of Pmc1p, a vacuolar v-SNARE protein, Nyv1p, was recovered. Cells overproducing Nyv1p show decreased Ca²⁺ tolerance and decreased accumulation of Ca²⁺ in the vacuole, similar to pmc1 null mutants. Overexpression of Nyv1p had no such effects on pmc1 mutants, suggesting that Nyv1p may inhibit Pmc1p function. Overexpression of Nyv1p did not decrease Pmc1p levels but decreased the specific ATP-dependent Ca²⁺ transport activity of Pmc1p in purified vacuoles by at least 2-fold. The effect of Nyv1p on Pmc1p function is likely to be direct because native immunoprecipitation experiments showed that Pmc1p coprecipitated with Nyv1p. Complexes between Nyv1p and its t-SNARE partner Vam3p were also isolated, but these complexes lacked Pmc1p. We conclude that Nyv1p can interact physically with Pmc1p and inhibit its Ca²⁺ transport activity in the vacuole membrane. This is the first example of a Ca²⁺-ATPase regulation by a v-SNARE protein involved in membrane fusion reactions.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				S. Sokolovski, A. Hills, R. A. Gay, and M. R. Blatt Functional Interaction of the SNARE Protein NtSyp121 in Ca2+ Channel Gating, Ca2+ Transients and ABA Signalling of Stomatal Guard Cells Mol Plant, March 1, 2008; 1(2): 347 - 358. [Abstract] [Full Text] [PDF]

				A. J. Merz and W. T. Wickner Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen J. Cell Biol., January 19, 2004; 164(2): 195 - 206. [Abstract] [Full Text] [PDF]