Maru Jaime-Garza

ORCID: 0000-0003-3612-1739
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About
Contact & Profiles
Research Areas
  • Endoplasmic Reticulum Stress and Disease
  • Heat shock proteins research
  • Parkinson's Disease Mechanisms and Treatments
  • Enzyme Structure and Function
  • Protein Structure and Dynamics
  • Fungal and yeast genetics research

University of California, San Francisco
2020-2023

QB3
2020

The Hsp90 molecular chaperone collaborates with the phosphorylated Cdc37 cochaperone for folding and activation of its many client kinases. As kinases, kinase CRaf is activated by phosphorylation at specific regulatory sites. phosphatase PP5 dephosphorylates in an Hsp90-dependent manner. Although dephosphorylating has been proposed as a mechanism releasing Hsp90-bound here we show that bound kinases sterically inhibit dephosphorylation indicating release must occur before dephosphorylation....

10.1038/s41467-023-37659-7 article EN cc-by Nature Communications 2023-04-17

Protein conformations are shaped by cellular environments, but how environmental changes alter the conformational landscapes of specific proteins in vivo remains largely uncharacterized, part due to challenge probing protein structures living cells. Here, we use deep mutational scanning investigate a toxic conformation α-synuclein, dynamic linked Parkinson's disease, responds perturbations proteostasis. In context course for graduate students UCSF Integrative Program Quantitative Biology,...

10.1021/acschembio.0c00339 article EN ACS Chemical Biology 2020-07-27

Abstract The Hsp90 molecular chaperone collaborates with the phosphorylated Cdc37 cochaperone to maintain kinase proteostasis through folding and activation of its many client kinases. As kinases, CRaf is activated by phosphorylation at specific regulatory sites. phosphatase PP5 dephosphorylates but also in an Hsp90-dependent manner. Although dephosphorylating has been proposed as a mechanism for releasing Hsp90-bound here we show that bound kinases sterically inhibit dephosphorylation...

10.1101/2022.09.02.506407 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2022-09-03

ABSTRACT Protein conformations are shaped by cellular environments, but how environmental changes alter the conformational landscapes of specific proteins in vivo remains largely uncharacterized, part due to challenge probing protein structures living cells. Here, we use deep mutational scanning investigate a toxic conformation α-synuclein, dynamic linked Parkinson’s disease, responds perturbations proteostasis. In context course for graduate students UCSF Integrative Program Quantitative...

10.1101/2020.05.01.072884 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-05-03
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