High impact information on Hsc70-1

• Consistent with this biochemical role, animals with reduced auxilin function exhibit genetic interactions with Hsc70 and clathrin [1].
• Thus, Rme-8 appears to function as an unexpected but critical cochaperone with Hsc70 in endocytosis [2].
• The sequence at the 5' and 3' junctions of the insertion is similar to that found in many intervening sequences. cDNA extension experiments indicate that the hsc70 gene is transcribed at normal temperatures in adult flies and that transcription is not enhanced by heat treatment [3].
• In vitro binding assays demonstrated direct interactions between CHIP and both Hsc70 and Hsp70, and complexes containing CHIP and Hsc70 were identified in immunoprecipitates of human skeletal muscle cells in vivo [4].
• The cysteine string secretory vesicle protein activates Hsc70 ATPase [5].

Biological context of Hsc70-1

• The sequences at the 5' and 3' junctions of the insertions in both Hsc1 and Hsc2 are similar to those found in intervening sequences of Drosophila and of many other organisms [6].
• Hsc70 is an abundant neural protein with coupled protein binding and ATPase activities [5].

Anatomical context of Hsc70-1

• Previous studies revealed multiple defects at neuromuscular junctions (NMJs) of csp null-mutant Drosophila, but whether these defects are independent of each other or mechanistically linked through J domain mediated-interactions with heat-shock cognate protein 70 (Hsc70) has not been established [7].

Other interactions of Hsc70-1

• However, in the codon specifying aa66 Hsc1 is interrupted by 1.7 kb of DNA; in the codon for aa55 Hsc2 contains an insertion of about 650 b [6].
• While transcripts from Hsc4 were equally abundant in RNA isolated from embryos, larvae and adults, Hsc1 and Hsc2 transcripts were not detected in embryo and larval RNA, and are therefore at least 20 times less abundant in these stages than in adults [6].

References