hsc 70
Recently Published Documents


TOTAL DOCUMENTS

27
(FIVE YEARS 0)

H-INDEX

15
(FIVE YEARS 0)

2016 ◽  
Vol 291 (35) ◽  
pp. 18096-18106 ◽  
Author(s):  
Kateryna Morozova ◽  
Cristina C. Clement ◽  
Susmita Kaushik ◽  
Barbara Stiller ◽  
Esperanza Arias ◽  
...  

Biochimie ◽  
2015 ◽  
Vol 108 ◽  
pp. 186-192 ◽  
Author(s):  
Ziming Zhang ◽  
Jason Cellitti ◽  
Peter Teriete ◽  
Maurizio Pellecchia ◽  
Boguslaw Stec

2010 ◽  
Vol 316 (16) ◽  
pp. 2692-2706 ◽  
Author(s):  
Esther Zumaquero ◽  
Pilar Muñoz ◽  
Marién Cobo ◽  
Gema Lucena ◽  
Esther J. Pavón ◽  
...  
Keyword(s):  
B Cells ◽  

2010 ◽  
Vol 76 (5) ◽  
pp. 857-864 ◽  
Author(s):  
Lung-Yin Hsu ◽  
Fu-Lung Yeh ◽  
Tun-Yuan Cheng ◽  
You-Hsin Chang ◽  
Shiu-Mei Liu ◽  
...  

2008 ◽  
Vol 19 (1) ◽  
pp. 405-413 ◽  
Author(s):  
Iris Rapoport ◽  
Werner Boll ◽  
Anan Yu ◽  
Till Böcking ◽  
Tom Kirchhausen

The 70-kDa heat-shock cognate protein (Hsc70) chaperone is an ATP-dependent “disassembly enzyme” for many subcellular structures, including clathrin-coated vesicles where it functions as an uncoating ATPase. Hsc70, and its cochaperone auxilin together catalyze coat disassembly. Like other members of the Hsp70 chaperone family, it is thought that ATP-bound Hsc70 recognizes the clathrin triskelion through an unfolded exposed hydrophobic segment. The best candidate is the unstructured C terminus (residues 1631–1675) of the heavy chain at the foot of the tripod below the hub, containing the sequence motif QLMLT, closely related to the sequence bound preferentially by the substrate groove of Hsc70 ( Fotin et al., 2004b ). To test this hypothesis, we generated in insect cells recombinant mammalian triskelions that in vitro form clathrin cages and clathrin/AP-2 coats exactly like those assembled from native clathrin. We show that coats assembled from recombinant clathrin are good substrates for ATP- and auxilin-dependent, Hsc70-catalyzed uncoating. Finally, we show that this uncoating reaction proceeds normally when the coats contain recombinant heavy chains truncated C-terminal to the QLMLT motif, but very inefficiently when the motif is absent. Thus, the QLMLT motif is required for Hsc-70–facilitated uncoating, consistent with the proposal that this sequence is a specific target of the chaperone.


2005 ◽  
Vol 328 (2) ◽  
pp. 550-559 ◽  
Author(s):  
Yoav E. Timsit ◽  
Stephanie L.H. Miller ◽  
Robert P. Mohney ◽  
John P. O’Bryan

Sign in / Sign up

Export Citation Format

Share Document