Role of chaperonin-like proteins in Bardet-Biedl syndrome / Michel R. Leroux.

Format:

Video

Author/Creator:

Leroux, Michel R., author.

Language:

English

Subjects (All):

Molecular chaperones.

Molecular chaperones--Physiological effect.

Physical Description:

1 videorecording (45 min., 30 sec.) : sound, color

Place of Publication:

London : Henry Stewart Talks, 2019.

System Details:

video file

Contents:

Introduction

Molecular chaperones: protein quality control

Group I and group II chaperonins

Structure of group I and group II chaperonins

Phylogenetic tree of group II chaperonins

Function of chaperonin containing TCP-1 (CCT)

Chaperonin CCT and disease

Cloning of chaperonin-like MKKS/BBS genes

Bardet-Biedl syndrome: pleiotropic, multigenic

Bardet-Biedl syndrome: a ciliopathy

Cilia are motile and sensory organelles

Motility and sensory roles of cilia

Ciliary disorders affect most organs

A chaperonin causes Bardet-Biedl syndrome

BBS6 is quickly-evolving protein related to CCT

BBS6 has unique biochemical properties

BBS6 is not associated with CCT

BBS6 is a novel centrosomal protein

BBS6 is centrosome-associated in cell cycle

BBS6 proteins from patients mislocalise (1)

BBS6 proteins from patients mislocalise (2)

Phenotypes of BBS6 knockdown by siRNA (1)

Phenotypes of BBS6 knockdown by siRNA (2)

BBS6 helps membrane fusion proteins bridge?

BBS6 mouse knockout

Two more chaperonin-like BBS proteins

Identification of chaperonin-like BBS10 gene

Identification of chaperonin-like BBS12 gene

Phylogenetic tree of CCT and BBS protein family

Sequence conservation of BBS proteins

BBS6, 10, 12 are atypical chaperonin proteins

Knockdown of bbs6 and bbs10 in zebrafish

Conclusions to date

Evolutionarily conserved BBS protein pathway

Roles for chaperonins in BBS protein pathway

Summary

Acknowledgments.

Notes:

Description based on publisher supplied metadata and other sources.

Retrieved April 19, 2024, from https://hstalks.com/bs/347/.