Off-campus UMass Amherst users: To download campus access dissertations, please use the following link to log into our proxy server with your UMass Amherst user name and password.

Non-UMass Amherst users: Please talk to your librarian about requesting this dissertation through interlibrary loan.

Dissertations that have an embargo placed on them will not be available to anyone until the embargo expires.

Author ORCID Identifier

https://orcid.org/0000-0001-5665-5098

AccessType

Open Access Dissertation

Document Type

dissertation

Degree Name

Doctor of Philosophy (PhD)

Degree Program

Molecular and Cellular Biology

Year Degree Awarded

2020

Month Degree Awarded

February

First Advisor

Daniel Hebert

Second Advisor

Dominique Alfandari

Third Advisor

Peter Chien

Fourth Advisor

Richard Vachet

Subject Categories

Animal Experimentation and Research | Biochemistry | Bioinformatics | Cell and Developmental Biology | Cell Biology | Developmental Biology | Integrative Biology | Molecular Biology | Other Animal Sciences

Abstract

The endoplasmic reticulum (ER) is a complex, multifunctional organelle comprised of a continuous membrane and lumen that is organized into several functional regions. It plays various roles including protein translocation, folding, quality control, secretion, calcium signaling, and lipid biogenesis. Cellular protein homeostasis is maintained by a complicated chaperone network, and the largest functional family within this network consists of proteins containing tetratricopeptide repeats (TPRs). TPRs are well-studied structural motifs that mediate intermolecular protein-protein interactions, supporting interactions with a wide range of ligands or substrates. Nine TPR-containing proteins have been shown to localize to the ER and control protein organization and homeostasis within this multifunctional organelle. Here, we discuss the roles of SEL1L, ERdj6, FICD, TMTC1-4, TTC13 and TTC17 and how they contribute to controlling ER processes and organization. The crucial roles that TPR-containing proteins play in the ER are highlighted by diseases or defects associated with their mutation or disruption.

DOI

https://doi.org/10.7275/3w2g-4r67

Share

COinS