N-ethylmaleimide sensitive factor (NSF) structure and function

S. W. Whiteheart, T. Schraw, E. A. Matveeva

Research output: Contribution to journalArticlepeer-review

103 Scopus citations


Our understanding of the molecular mechanisms of membrane trafficking advanced at a rapid rate during the 1990s. As one of the initial protein components of the trafficking machinery to be identified, N-ethylmaleimide sensitive factor (NSF) has served as a reference point in many of these recent studies. This hexameric ATPase is essential for most of the membrane-trafficking events in a cell. Initially, due to its ATPase activity, NSF was thought to be the motor that drove membrane fusion. Subsequent studies have shown that NSF actually plays the role of a chaperone by activating SNAP receptor proteins (SNAREs) so that they can participate in membrane fusion. In this review we will examine the initial characterization of NSF, its role in membrane fusion events, and what new structural information can tell us about NSF's mechanism of action.

Original languageEnglish
Pages (from-to)71-112
Number of pages42
JournalInternational Review of Cytology
StatePublished - 2001

Bibliographical note

Funding Information:
We would like to thank Dr. Susan Buhrow for her expert comments on this manuscript. We would also like to acknowledge the stimulating comments of members of the Whiteheart laboratory: Dr. Dong Chen, Tara Rutledge, and Ping He. This work is supported by a grant from the National Heart Lung and Blood Institute of the National Institutes of Health.


  • AAA proteins
  • ATPase
  • Exocytosis
  • NSF
  • SNAPs
  • SNAREs
  • Secretion
  • Vesicular transport

ASJC Scopus subject areas

  • Histology
  • Cell Biology


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