Putative tyrosine-protein phosphatase auxilin is an enzyme that in humans is encoded by the DNAJC6 gene. [5][6][7] DNAJC6 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity.

We named the putative auxilin homologs AUXILIN-LIKE1 (AT4G12780) and AUXILIN-LIKE2 (AT4G12770). These two proteins belong to a family of seven proteins in Arabidopsis with C-terminal DNAJ domains, which can all therefore be called auxilin-likes.

Perhaps the best-studied J-domain-protein model system (at the biochemical level) is auxilin, a co-chaperone that, together with an Hsp70, uncoats clathrin-coated vesicles in an in vitro system composed entirely of purified components [9].

Oct 24, 2004 · Auxilin binding produces a local change in heavy-chain contacts, creating a detectable global distortion of the clathrin coat. We propose a mechanism by which local destabilization of the...

Jan 23, 2001 · The DnaJ protein auxilin has been extensively studied in vitro as a cofactor for uncoating clathrin-coated vesicles by the chaperone Hsc70. Recent studies provide the first evidence that auxilin plays this role in vivo, and work on a new mammalian auxilin suggests the protein may have more complex cellular functions.

We propose for the new protein the name auxilin (Latin auxilium, meaning support). Auxilin migrates as a 110-kD polypeptide in standard type SDS-PAGE, but in the presence of 6 M urea shifts to a position corresponding to 126 kD.

Jan 1, 2016 · We describe a proteomic and genetic approach that connects the J-domain chaperone auxilin, which uncoats clathrin-coated vesicles, to COPII and COPI coat complexes. Consistent with a functional role for auxilin in the early secretory pathway, auxilin binds to COPII and COPI coat subunits.

May 10, 2022 · Here, we find that auxilin (Aux) restricts intestinal stem cell (ISC) proliferation mainly through EGFR signaling. aux depletion leads to excessive ISC proliferation and midgut homeostasis disruption, which is unlikely caused by defective Notch signaling.

Mar 2, 2020 · Clathrin-coated vesicles lose their clathrin lattice within seconds of pinching off, through the action of the Hsc70 "uncoating ATPase." The J- and PTEN-like domain-containing proteins, auxilin 1 (Aux1) and auxilin 2 (GAK), recruit Hsc70.

Two proteins that may play a major role in this process are Hsc70 and its cochaperones, either the neuronally expressed auxilin or the ubiquitously expressed GAK, which is an acronym for cyclin-G–associated kinase.