Uncoating ATPase is a member of the 70 kilodalton family of stress proteins

Sorting and processing of secretory proteins

“…The maturation of secretory granules involves not only progressive acidification and prohormone conversion but also the loss of the clathrin coat [71,72]. Clathrin is removed from coated vesicles by disassembly mediated by an ATP-dependent uncoating enzyme [73] shown to be a member of the 70 kDa family of stress proteins [74]. It is not yet known whether the same mechanism is responsible for the uncoating of secretory granules.…”

Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly and Membrane Translocation of Proteins

“…Interaction of hsp70 proteins has been described in the literature with a large number of diverse proteins including: clathrin (UNGEWICKELL 1985;CHAPPELL et al 1986); the cellular proto-oncogene p53 (PINHASI-KIMHI et al 1986); certain trans-activating proteins such as E1a of adenovirus (WALTER et al 1987); malfolded or incompletely assembled proteins in the ER (with BiP, see below);…”

“…Immunological cross-reactivity, peptide mapping and two-dimensional gel analysis identified the uncoating ATPase as a constitutively synthesized member of the hsp70 family, called hsc70 (UNGEWICKELL 1985;CHAPPELL et al 1986). …”

Escherichia coli DnaK and GrpE heat shock proteins interact both in vivo and in vitro

“…This 70-kilodalton protein shows approximately 50% amino acid identity with the Hsp7O family of proteins present in all cells examined (4, 9, 21). DnaK and its eucaryotic homologs appear to mediate protein stabilization, refolding, and dissociation (6,19,26). As an example, during initiation of A DNA replication, the DnaK and DnaJ HS proteins, which are essential for A DNA replication, catalyze the ATP-dependent dissociation of A P protein from a complex which includes the X 0, A P, and E. coli DnaB proteins assembled at oriA (20).…”