Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface

Jianwen Jiang, Alexander B. Taylor, Kondury Prasad, Yumiko Ishikawa-Brush, Peter J Hart, Eileen M. Lafer, Rui J Sousa

Research output: Contribution to journalArticlepeer-review

47 Scopus citations


J-domains are widespread protein interaction modules involved in recruiting and stimulating the activity of Hsp70 family chaperones. We have determined the crystal structure of the J-domain of auxilin, a protein which is involved in uncoating clathrin-coated vesicles. Comparison to the known structures of J-domains from four other proteins reveals that the auxilin J-domain is the most divergent of all J-domain structures described to date. In addition to the canonical J-domain features described previously, the auxilin J-domain contains an extra N-terminal helix and a long loop inserted between helices I and II. The latter loop extends the positively charged surface which forms the Hsc70 binding site, and is shown by directed mutagenesis and surface plasmon resonance to contain side chains important for binding to Hsc70.

Original languageEnglish (US)
Pages (from-to)5748-5753
Number of pages6
Issue number19
StatePublished - May 20 2003

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface'. Together they form a unique fingerprint.

Cite this