Roles for molecular chaperones in cystic fibrosis / Douglas M. Cyr.

Format:

Video

Author/Creator:

Cyr, Douglas M., author.

Language:

English

Subjects (All):

Cystic fibrosis.

Molecular chaperones.

Physical Description:

1 streaming video file (53 min.) : digital, mono, SWF file, sound, color

Place of Publication:

London : Henry Stewart Talks Ltd, 2007.

System Details:

video file

Summary:

Audio-visual presentation : Cystic fibrosis is a fatal homozygous recessive disorder ; Caused primarily by misfolding of mutant forms of cystic fibrosis transmembrane conductance regulator (CFTR) ; The folding defects in mutant CFTR are detected by protein quality control machines in the endoplasmic reticulum that target mutant CFTR for premature degradation ; Small molecules that are being developed as drugs to treat cystic fibrosis enable mutant CFTR to avoid recognition by the endoplasmic reticulum quality control system and function at the cell surface.

Contents:

Introduction

CFTR protein and its mutations in CF patients

Mislocalization of deltaF508 CFTR

Consequences of defects in CFTR function

CFTR activity correlates with CF severity

Cystic fibrosis foundation therapeutics pipeline

CF and CFTR folding/degradation

Role of chaperones in CFTR biogenesis

Results of calnexin inactivation

Results of Hsc70 inactivation

Regulation of Hsp70 function by Hsp40

Type I Hsp40 proteins contain a CAAX box

Steps in the CFTR folding pathway

Does Hsc70 facilitate CFTR degradation?

U-box family

Results of CHIP overexpression

CHIP expression blocks CFTR processing

CHIP mediated triage of misfolded proteins

CFTR-deltaF508 partitioning between pathways

RMA1 is an ER localized RING E3

Elevation of Rma1 levels blocks CFTR folding

Results of Rma1 and Ubc6e reduction

E2/E3 ubiquitin ligase senses folded CFTR

Derlin-1 protein

Results of DER1 overexpression

Results of DER1 knockdown

Possible role of DER1

CFTR-deltaF508 sensitivity to Rma1 changes

Regions recognized by Rma1 and CHIP E3

Sensing delta-F508 folding defects

CFTR sub-domains recognition by Rma1/CHIP

Small molecules and CFTR folding efficiency

Results of treatment with VRT-532 and Corr4a

Recognition of CFTR-deltaF508 folding defects

Acknowledgements.

Notes:

Description based on publisher supplied metadata and other sources.

Retrieved April 16, 2024, from https://hstalks.com/bs/349/.