Literature DB >> 31732684

New gadget in the membrane trafficking toolbox: A novel inhibitor of SNARE priming.

Hagai Abeliovich1.   

Abstract

NSF (N-ethylmaleimide sensitive factor) and its yeast counterpart Sec18 are highly conserved homohexameric proteins that play vital roles in eukaryotic membrane trafficking. Sec18 functions by disrupting SNARE complexes formed in cis, on the same membrane. However, the molecular mechanisms of this process are poorly understood, in large part due to the lack of selective, reversible inhibitors. A new study by Sparks et al. now reports a small molecule that appears to selectively inhibit Sec18 action in an in vitro assay. Their finding now paves the way to elucidate further details of Sec18-mediated SNARE priming.
© 2019 Abeliovich.

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Year:  2019        PMID： 31732684      PMCID： PMC6873167          DOI： 10.1074/jbc.H119.011334

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  11 in total

1.  The principle of membrane fusion in the cell (Nobel lecture).

Authors:  James Edward Rothman
Journal:  Angew Chem Int Ed Engl       Date:  2014-08-01       Impact factor: 15.336

2.  Possible role for fatty acyl-coenzyme A in intracellular protein transport.

Authors:  B S Glick; J E Rothman
Journal:  Nature       Date:  1987 Mar 19-25       Impact factor: 49.962

3.  Phosphatidic acid induces conformational changes in Sec18 protomers that prevent SNARE priming.

Authors:  Matthew L Starr; Robert P Sparks; Andres S Arango; Logan R Hurst; Zhiyu Zhao; Muyun Lihan; Jermaine L Jenkins; Emad Tajkhorshid; Rutilio A Fratti
Journal:  J Biol Chem       Date:  2019-01-07       Impact factor: 5.157

4.  Characterization of a component of the yeast secretion machinery: identification of the SEC18 gene product.

Authors:  K A Eakle; M Bernstein; S D Emr
Journal:  Mol Cell Biol       Date:  1988-10       Impact factor: 4.272

5.  A revised model for the oligomeric state of the N-ethylmaleimide-sensitive fusion protein, NSF.

Authors:  K G Fleming; T M Hohl; R C Yu; S A Müller; B Wolpensinger; A Engel; H Engelhardt; A T Brünger; T H Söllner; P I Hanson
Journal:  J Biol Chem       Date:  1998-06-19       Impact factor: 5.157

6.  Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport.

Authors:  M R Block; B S Glick; C A Wilcox; F T Wieland; J E Rothman
Journal:  Proc Natl Acad Sci U S A       Date:  1988-11       Impact factor: 11.205

Review 7.  Review: Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes.

Authors:  Je-Kyung Ryu; Reinhard Jahn; Tae-Young Yoon
Journal:  Biopolymers       Date:  2016-08       Impact factor: 2.505

8.  Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway.

Authors:  P Novick; C Field; R Schekman
Journal:  Cell       Date:  1980-08       Impact factor: 41.582

9.  A small-molecule competitive inhibitor of phosphatidic acid binding by the AAA+ protein NSF/Sec18 blocks the SNARE-priming stage of vacuole fusion.

Authors:  Robert P Sparks; Andres S Arango; Matthew L Starr; Zachary L Aboff; Logan R Hurst; David A Rivera-Kohr; Chi Zhang; Kevin A Harnden; Jermaine L Jenkins; Wayne C Guida; Emad Tajkhorshid; Rutilio A Fratti
Journal:  J Biol Chem       Date:  2019-09-12       Impact factor: 5.486

10.  A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion.

Authors:  C Ungermann; B J Nichols; H R Pelham; W Wickner
Journal:  J Cell Biol       Date:  1998-01-12       Impact factor: 10.539
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