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The following terms were not found in PubMed: LOC105378189, LOC105378189
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mTOR-mediated phosphorylation of VAMP8 and SCFD1 regulates autophagosome maturation.
Huang H, Ouyang Q, Zhu M, Yu H, Mei K, Liu R. Huang H, et al. Nat Commun. 2021 Nov 16;12(1):6622. doi: 10.1038/s41467-021-26824-5. Nat Commun. 2021. PMID: 34785650 Free PMC article.
Furthermore, we identify SCFD1, a Sec1/Munc18-like protein, that localizes to the autolysosome and is required for SNARE complex formation and autophagosome-lysosome fusion. VAMP8 promotes SCFD1 recruitment to autolysosomes when dephosphorylated. Consistently …
Furthermore, we identify SCFD1, a Sec1/Munc18-like protein, that localizes to the autolysosome and is required for SNARE complex form …
Mammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to Golgi transport.
Dascher C, Balch WE. Dascher C, et al. J Biol Chem. 1996 Jul 5;271(27):15866-9. doi: 10.1074/jbc.271.27.15866. J Biol Chem. 1996. PMID: 8663406 Free article.
Members of the syntaxin gene family are components of protein complexes which regulate vesicle docking and/or fusion during transport of cargo through the secretory pathway of eukaryotic cells. ...We demonstrate that this protein is the mammalian homologue to yeast Sly1p, …
Members of the syntaxin gene family are components of protein complexes which regulate vesicle docking and/or fusion during transport …
SLY1 and Syntaxin 18 specify a distinct pathway for procollagen VII export from the endoplasmic reticulum.
Nogueira C, Erlmann P, Villeneuve J, Santos AJ, Martínez-Alonso E, Martínez-Menárguez JÁ, Malhotra V. Nogueira C, et al. Elife. 2014 May 19;3:e02784. doi: 10.7554/eLife.02784. Elife. 2014. PMID: 24842878 Free PMC article.
In this study, we report a connection between the cytoplasmic domain of TANGO1 and SLY1, a protein that is required for membrane fusion. Knockdown of SLY1 by siRNA arrested Procollagen VII in the ER without affecting the recruitment of COPII components, general protein sec …
In this study, we report a connection between the cytoplasmic domain of TANGO1 and SLY1, a protein that is required for membrane fusion …
Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing.
Laufman O, Kedan A, Hong W, Lev S. Laufman O, et al. EMBO J. 2009 Jul 22;28(14):2006-17. doi: 10.1038/emboj.2009.168. Epub 2009 Jun 18. EMBO J. 2009. PMID: 19536132 Free PMC article.
The crucial roles of Sec1/Munc18 (SM)-like proteins in membrane fusion have been evidenced in genetic and biochemical studies. SM proteins interact directly with SNAREs and contribute to SNARE pairing by a yet unclear mechanism. ...
The crucial roles of Sec1/Munc18 (SM)-like proteins in membrane fusion have been evidenced in genetic and biochemical studies. SM pro …
Mutations of the SM protein Sly1 resulting in bypass of GTPase requirement in vesicular transport are confined to a short helical region.
Li Y, Schmitt HD, Gallwitz D, Peng RW. Li Y, et al. FEBS Lett. 2007 Dec 11;581(29):5698-702. doi: 10.1016/j.febslet.2007.11.033. Epub 2007 Nov 26. FEBS Lett. 2007. PMID: 18036347 Free article.
Ypt/Rab GTPases and Sec1/Munc18 (SM) proteins are key components of the membrane fusion machinery. Here, we describe new mutants of the yeast SM protein Sly1 that specifically bypass the need for GTPases Ypt1 and Ypt6 in vesicular transport. ...This indicates that alpha-20 …
Ypt/Rab GTPases and Sec1/Munc18 (SM) proteins are key components of the membrane fusion machinery. Here, we describe new mutants of t …