High impact information on DNAJC6

• Role of auxilin in uncoating clathrin-coated vesicles [1].
• Uncoating of clathrin-coated vesicles in presynaptic terminals: roles for Hsc70 and auxilin [2].
• Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin [3].
• Auxilin, a newly identified clathrin-associated protein in coated vesicles from bovine brain [4].
• 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 [4].

Biological context of DNAJC6

• The combined open reading frames of three cow brain cDNA clones with a total of 4531 nucleotides predict a molecular mass of 99,504 Da for auxilin [5].
• We have examined the roles of Hsc70 and auxilin in the uncoating of clathrin-coated vesicles (CCVs) during neuronal endocytosis [2].

Anatomical context of DNAJC6

• We have determined the crystal structure of the J-domain of auxilin, a protein which is involved in uncoating clathrin-coated vesicles [6].
• These studies establish that auxilin and Hsc70 participate in synaptic vesicle recycling in neurons and that an interaction between these proteins is required for CCV uncoating [2].

Associations of DNAJC6 with chemical compounds

• A detailed sequence comparison indicates that the PTP-like domain in tensin is unlikely to exhibit phosphatase activity, whereas in auxilin it may possess a different phosphatase specificity from tyrosine phosphatases [7].

Regulatory relationships of DNAJC6

• Auxilin also induced polymerization of Hsc70 and bound to the resulting polymer at a 1:1 molar ratio; here too the dissociation constant was 0.6 microM [8].

Other interactions of DNAJC6

• The Hsc70 molecular chaperone effects the uncoating reaction, and is guided to appropriate locations on clathrin lattices by the J-domain-containing co-chaperone molecule auxilin [9].

Analytical, diagnostic and therapeutic context of DNAJC6

• Recombinant auxilin expressed in and purified from bacteria by affinity chromatography is functional with respect to clathrin binding [5].
• Here, we have used electron cryomicroscopy to determine 12-A-resolution structures of in-vitro-assembled clathrin coats in association with a carboxy-terminal fragment of auxilin that contains both the clathrin-binding region and the J domain [9].
• Immunoblotting did not reveal the presence of auxilin in tissues other than brain [4].
• We find that during coat assembly small and variable amounts of auxilin are recruited transiently but that a much larger burst of association occurs after the peak of dynamin signal, during the transition between membrane constriction and vesicle budding [10].

References