Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif

The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the... FYVE and coiled‐coil domain‐containing protein 1 (FYCO1), a multidomain autophagy adaptor protein, mediates microtubule plus‐end‐directed autophagosome transport by interacting with kinesin motor proteins and with the autophagosomal membrane components microtubule‐associated protein 1 light chain 3 (LC3), Rab7 and phosphatidylinositol 3‐phosphate (PI3P). To establish the structural basis for the recognition of FYCO1 by LC3, the crystal structure of mouse LC3B in complex with the FYCO1 LC3‐interacting region (LIR) motif peptide was determined. Structural analysis showed that the flanking sequences N‐terminal and C‐terminal to the LIR core sequence of FYCO1, as well as the tetrapeptide core sequence, were specifically recognized by LC3B and contributed to the binding. Moreover, comparisons of related structures revealed a conserved mechanism of FYCO1 recognition by different LC3 isoforms among different species. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif

Loading next page...
 
/lp/wiley/the-crystal-structure-of-mouse-lc3b-in-complex-with-the-fyco1-lir-m2AESbbI6L

References (39)

Publisher
Wiley
Copyright
Copyright © 2017 Wiley Subscription Services
ISSN
2053-230X
eISSN
2053-230X
DOI
10.1107/S2053230X17001911
pmid
28291748
Publisher site
See Article on Publisher Site

Abstract

FYVE and coiled‐coil domain‐containing protein 1 (FYCO1), a multidomain autophagy adaptor protein, mediates microtubule plus‐end‐directed autophagosome transport by interacting with kinesin motor proteins and with the autophagosomal membrane components microtubule‐associated protein 1 light chain 3 (LC3), Rab7 and phosphatidylinositol 3‐phosphate (PI3P). To establish the structural basis for the recognition of FYCO1 by LC3, the crystal structure of mouse LC3B in complex with the FYCO1 LC3‐interacting region (LIR) motif peptide was determined. Structural analysis showed that the flanking sequences N‐terminal and C‐terminal to the LIR core sequence of FYCO1, as well as the tetrapeptide core sequence, were specifically recognized by LC3B and contributed to the binding. Moreover, comparisons of related structures revealed a conserved mechanism of FYCO1 recognition by different LC3 isoforms among different species.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2017

Keywords: ; ; ;

There are no references for this article.