Literature DB >> 16111939

Sec16 is a determinant of transitional ER organization.

Pamela L Connerly1, Masatoshi Esaki, Elisabeth A Montegna, Daniel E Strongin, Stephanie Levi, Jon Soderholm, Benjamin S Glick.   

Abstract

BACKGROUND: Proteins are exported from the ER at transitional ER (tER) sites, which produce COPII vesicles. However, little is known about how COPII components are concentrated at tER sites. The budding yeast Pichia pastoris contains discrete tER sites and is, therefore, an ideal system for studying tER organization.
RESULTS: We show that the integrity of tER sites in P. pastoris requires the peripheral membrane protein Sec16. P. pastoris Sec16 is an order of magnitude less abundant than a COPII-coat protein at tER sites and seems to show a saturable association with these sites. A temperature-sensitive mutation in Sec16 causes tER fragmentation at elevated temperature. This effect is specific because when COPII assembly is inhibited with a dominant-negative form of the Sar1 GTPase, tER sites remain intact. The tER fragmentation in the sec16 mutant is accompanied by disruption of Golgi stacks.
CONCLUSIONS: Our data suggest that Sec16 helps to organize patches of COPII-coat proteins into clusters that represent tER sites. The Golgi disruption that occurs in the sec16 mutant provides evidence that Golgi structure in budding yeasts depends on tER organization.

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Year:  2005        PMID: 16111939     DOI: 10.1016/j.cub.2005.06.065

Source DB:  PubMed          Journal:  Curr Biol        ISSN: 0960-9822            Impact factor:   10.834


  75 in total

Review 1.  COPII and the regulation of protein sorting in mammals.

Authors:  Giulia Zanetti; Kanika Bajaj Pahuja; Sean Studer; Soomin Shim; Randy Schekman
Journal:  Nat Cell Biol       Date:  2011-12-22       Impact factor: 28.824

2.  Dual function of Sec16B: Endoplasmic reticulum-derived protein secretion and peroxisome biogenesis in mammalian cells.

Authors:  Katsuko Tani; Mitsuo Tagaya; Shusuke Yonekawa; Takashi Baba
Journal:  Cell Logist       Date:  2011-07-01

Review 3.  The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.

Authors:  Stephanie K Levi; Dibyendu Bhattacharyya; Rita L Strack; Jotham R Austin; Benjamin S Glick
Journal:  Traffic       Date:  2010-06-21       Impact factor: 6.215

4.  The secretory system of Arabidopsis.

Authors:  Diane C Bassham; Federica Brandizzi; Marisa S Otegui; Anton A Sanderfoot
Journal:  Arabidopsis Book       Date:  2008-09-30

5.  Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization.

Authors:  Dibyendu Bhattacharyya; Benjamin S Glick
Journal:  Mol Biol Cell       Date:  2006-12-27       Impact factor: 4.138

Review 6.  Protein energetics in maturation of the early secretory pathway.

Authors:  R Luke Wiseman; Atanas Koulov; Evan Powers; Jeffery W Kelly; William E Balch
Journal:  Curr Opin Cell Biol       Date:  2007-08-07       Impact factor: 8.382

7.  STAM adaptor proteins interact with COPII complexes and function in ER-to-Golgi trafficking.

Authors:  Neggy Rismanchi; Rosa Puertollano; Craig Blackstone
Journal:  Traffic       Date:  2008-11-18       Impact factor: 6.215

Review 8.  Regulation of traffic and organelle architecture of the ER-Golgi interface by signal transduction.

Authors:  Kerstin D Tillmann; Valentina Millarte; Hesso Farhan
Journal:  Histochem Cell Biol       Date:  2013-07-03       Impact factor: 4.304

Review 9.  Retrograde traffic from the Golgi to the endoplasmic reticulum.

Authors:  Anne Spang
Journal:  Cold Spring Harb Perspect Biol       Date:  2013-06-01       Impact factor: 10.005

10.  MAIGO5 functions in protein export from Golgi-associated endoplasmic reticulum exit sites in Arabidopsis.

Authors:  Junpei Takagi; Luciana Renna; Hideyuki Takahashi; Yasuko Koumoto; Kentaro Tamura; Giovanni Stefano; Yoichiro Fukao; Maki Kondo; Mikio Nishimura; Tomoo Shimada; Federica Brandizzi; Ikuko Hara-Nishimura
Journal:  Plant Cell       Date:  2013-11-26       Impact factor: 11.277

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