Structure and membrane remodeling activity of ESCRT-III helical polymers-Reference-Cited by-同舟云学术

Structure and membrane remodeling activity of ESCRT-III helical polymers

Published:2015-12-18 Issue:6267 Volume:350 Page:1548-1551
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

McCullough John¹,Clippinger Amy K.²,Talledge Nathaniel¹³,Skowyra Michael L.²,Saunders Marissa G.¹,Naismith Teresa V.²,Colf Leremy A.¹,Afonine Pavel⁴,Arthur Christopher⁵,Sundquist Wesley I.¹,Hanson Phyllis I.²,Frost Adam¹³

Affiliation:

1. Department of Biochemistry, University of Utah, Salt Lake City, UT 84112, USA.

2. Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, USA.

3. Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.

4. Physical Bioscience Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

5. FEI Company, Hillsboro, OR 97124, USA.

Abstract

ESCRTs work in two very different ways The so-called ESCRT proteins are involved in the budding of vesicles into the lumen of endosomes and in virus budding. These reactions involve the formation of a cytoplasm-filled neck that spirals of the ESCRTs help to seal. McCullough et al. now show that ESCRTs can also promote the scission of membrane tubules with the completely opposite topology. ESCRT-III and IST1 ESCRT subunits form spirals on the outside of membrane tubules and so can mediate the budding of tubules and vesicles into the cytosol. Relatively minor structural rearrangements were required to turn ESCRT function on its head. Science , this issue p. 1548

Funder

NSF

NIH

U.S. Department of Energy

American Cancer Society

Jane Coffin Childs Foundation

Searle Scholars Program

Phenix Industrial Consortium

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary