Structural basis for recognition of acidic-cluster dileucine sequence by GGA1 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-02

AUTHORS

Tomoo Shiba, Hiroyuki Takatsu, Terukazu Nogi, Naohiro Matsugaki, Masato Kawasaki, Noriyuki Igarashi, Mamoru Suzuki, Ryuichi Kato, Thomas Earnest, Kazuhisa Nakayama, Soichi Wakatsuki

ABSTRACT

GGAs (Golgi-localizing, γ-adaptin ear homology domain, ARF-interacting proteins) are critical for the transport of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF), and clathrin1,2. The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster dileucine (ACLL) sequences1,2,3,4,5,6. Here we report the X-ray structure of the GGA1 VHS domain alone, and in complex with the carboxy-terminal peptide of cation-independent mannose 6-phosphate receptor containing an ACLL sequence. The VHS domain forms a super helix with eight α-helices, similar to the VHS domains of TOM1 and Hrs. Unidirectional movements of helices α6 and α8, and some of their side chains, create a set of electrostatic and hydrophobic interactions for correct recognition of the ACLL peptide. This recognition mechanism provides the basis for regulation of protein transport from the TGN to endosomes/lysosomes, which is shared by sortilin and low-density lipoprotein receptor-related protein. More... »

PAGES

937-941

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/415937a

DOI

http://dx.doi.org/10.1038/415937a

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1047289235

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11859376


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