Sar1 assembly regulates membrane constriction and ER export.

Journal Article (Journal Article)

The guanosine triphosphatase Sar1 controls the assembly and fission of COPII vesicles. Sar1 utilizes an amphipathic N-terminal helix as a wedge that inserts into outer membrane leaflets to induce vesicle neck constriction and control fission. We hypothesize that Sar1 organizes on membranes to control constriction as observed with fission proteins like dynamin. Sar1 activation led to membrane-dependent oligomerization that transformed giant unilamellar vesicles into small vesicles connected through highly constricted necks. In contrast, membrane tension provided through membrane attachment led to organization of Sar1 in ordered scaffolds that formed rigid, uniformly nonconstricted lipid tubules to suggest that Sar1 organization regulates membrane constriction. Sar1 organization required conserved residues located on a unique C-terminal loop. Mutations in this loop did not affect Sar1 activation or COPII recruitment and enhanced membrane constriction, yet inhibited Sar1 organization and procollagen transport from the endoplasmic reticulum (ER). Sar1 activity was directed to liquid-disordered lipid phases. Thus, lipid-directed and tether-assisted Sar1 organization controls membrane constriction to regulate ER export.

Full Text

Duke Authors

Cited Authors

  • Long, KR; Yamamoto, Y; Baker, AL; Watkins, SC; Coyne, CB; Conway, JF; Aridor, M

Published Date

  • July 12, 2010

Published In

Volume / Issue

  • 190 / 1

Start / End Page

  • 115 - 128

PubMed ID

  • 20624903

Pubmed Central ID

  • PMC2911667

Electronic International Standard Serial Number (EISSN)

  • 1540-8140

Digital Object Identifier (DOI)

  • 10.1083/jcb.201004132


  • eng

Conference Location

  • United States