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Molecular interactions position Mso1p, a novel PTB domain homologue, in the interface of the exocyst complex and the exocytic SNARE machinery in yeast.

Knop M, Miller KJ, Mazza M, Feng D, Weber M, Keränen S, Jäntti J.

Mol Biol Cell. 2005 Oct;16(10):4543-56. Epub 2005 Jul 19.


A conserved regulatory mode in exocytic membrane fusion revealed by Mso1p membrane interactions.

Weber-Boyvat M, Zhao H, Aro N, Yuan Q, Chernov K, Peränen J, Lappalainen P, Jäntti J.

Mol Biol Cell. 2013 Feb;24(3):331-41. doi: 10.1091/mbc.E12-05-0415. Epub 2012 Nov 28.


Sec1p and Mso1p C-terminal tails cooperate with the SNAREs and Sec4p in polarized exocytosis.

Weber-Boyvat M, Aro N, Chernov KG, Nyman T, Jäntti J.

Mol Biol Cell. 2011 Jan 15;22(2):230-44. doi: 10.1091/mbc.E10-07-0592. Epub 2010 Nov 30.


Mso1p regulates membrane fusion through interactions with the putative N-peptide-binding area in Sec1p domain 1.

Weber M, Chernov K, Turakainen H, Wohlfahrt G, Pajunen M, Savilahti H, Jäntti J.

Mol Biol Cell. 2010 Apr 15;21(8):1362-74. doi: 10.1091/mbc.E09-07-0546. Epub 2010 Feb 24.


Sec1p binds to SNARE complexes and concentrates at sites of secretion.

Carr CM, Grote E, Munson M, Hughson FM, Novick PJ.

J Cell Biol. 1999 Jul 26;146(2):333-44.


Mso1 is a novel component of the yeast exocytic SNARE complex.

Castillo-Flores A, Weinberger A, Robinson M, Gerst JE.

J Biol Chem. 2005 Oct 7;280(40):34033-41. Epub 2005 Aug 8.


Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p.

Wiederkehr A, De Craene JO, Ferro-Novick S, Novick P.

J Cell Biol. 2004 Dec 6;167(5):875-87.


Interactions between Rabs, tethers, SNAREs and their regulators in exocytosis.

Novick P, Medkova M, Dong G, Hutagalung A, Reinisch K, Grosshans B.

Biochem Soc Trans. 2006 Nov;34(Pt 5):683-6.


Characterization of the sec1-1 and sec1-11 mutations.

Brummer MH, Kivinen KJ, Jäntti J, Toikkanen J, Söderlund H, Keränen S.

Yeast. 2001 Dec;18(16):1525-36.


Mso1p: a yeast protein that functions in secretion and interacts physically and genetically with Sec1p.

Aalto MK, Jäntti J, Ostling J, Keränen S, Ronne H.

Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7331-6.


Yeast Sec1p functions before and after vesicle docking.

Hashizume K, Cheng YS, Hutton JL, Chiu CH, Carr CM.

Mol Biol Cell. 2009 Nov;20(22):4673-85. doi: 10.1091/mbc.E09-02-0172. Epub 2009 Sep 23.


The yeast par-1 homologs kin1 and kin2 show genetic and physical interactions with components of the exocytic machinery.

Elbert M, Rossi G, Brennwald P.

Mol Biol Cell. 2005 Feb;16(2):532-49. Epub 2004 Nov 24.


The polybasic juxtamembrane region of Sso1p is required for SNARE function in vivo.

Van Komen JS, Bai X, Rodkey TL, Schaub J, McNew JA.

Eukaryot Cell. 2005 Dec;4(12):2017-28.


Ordering the final events in yeast exocytosis.

Grote E, Carr CM, Novick PJ.

J Cell Biol. 2000 Oct 16;151(2):439-52.


The polarity-establishment component Bem1p interacts with the exocyst complex through the Sec15p subunit.

France YE, Boyd C, Coleman J, Novick PJ.

J Cell Sci. 2006 Mar 1;119(Pt 5):876-88. Epub 2006 Feb 14.


Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1.

Morgera F, Sallah MR, Dubuke ML, Gandhi P, Brewer DN, Carr CM, Munson M.

Mol Biol Cell. 2012 Jan;23(2):337-46. doi: 10.1091/mbc.E11-08-0670. Epub 2011 Nov 23.


Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion.

Grote E, Baba M, Ohsumi Y, Novick PJ.

J Cell Biol. 2000 Oct 16;151(2):453-66.


Lethal giant larvae proteins interact with the exocyst complex and are involved in polarized exocytosis.

Zhang X, Wang P, Gangar A, Zhang J, Brennwald P, TerBush D, Guo W.

J Cell Biol. 2005 Jul 18;170(2):273-83.


Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis.

Rossi G, Brennwald P.

Mol Biol Cell. 2011 Mar 15;22(6):842-57. doi: 10.1091/mbc.E10-07-0570. Epub 2011 Jan 19.

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