Unknown

Dataset Information

0

The remarkable multivalency of the Hsp70 chaperones.


ABSTRACT: Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases.

SUBMITTER: Zuiderweg ER 

PROVIDER: S-EPMC5352603 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

The remarkable multivalency of the Hsp70 chaperones.

Zuiderweg Erik R P ER   Hightower Lawrence E LE   Gestwicki Jason E JE  

Cell stress & chaperones 20170220 2


Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active  ...[more]

Similar Datasets

| S-EPMC2773841 | biostudies-literature
| S-EPMC4595643 | biostudies-literature
| S-EPMC6369297 | biostudies-literature
| S-EPMC8500941 | biostudies-literature
| S-EPMC4753570 | biostudies-literature
| S-EPMC2964120 | biostudies-literature
| S-EPMC7219557 | biostudies-literature
| S-EPMC2693909 | biostudies-literature
| S-EPMC6747426 | biostudies-literature
| S-EPMC3483142 | biostudies-literature