TTC17 is an endoplasmic reticulum resident TPR-containing adaptor protein.

ER quality control TPR UGGT adaptor protein cell compartmentalization chaperone endoplasmic reticulum (ER) endoplasmic reticulum stress (ER stress) intracellular trafficking molecular chaperones protein trafficking secretion

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
08 Nov 2023
Historique:
received: 18 07 2023
revised: 11 10 2023
accepted: 29 10 2023
pubmed: 11 11 2023
medline: 11 11 2023
entrez: 10 11 2023
Statut: aheadofprint

Résumé

Protein folding, quality control, maturation, and trafficking are essential processes for proper cellular homeostasis. Around one-third of the human proteome is targeted to the endoplasmic reticulum (ER), the organelle that serves as entrance into the secretory pathway. Successful protein trafficking is paramount for proper cellular function and to that end there are many ER resident proteins that ensure efficient secretion. Here, biochemical and cell biological analysis was used to determine that TTC17 is a large, soluble, ER-localized protein that plays an important role in secretory trafficking. Transcriptional analysis identified the predominantly expressed protein isoform of TTC17 in various cell lines. Further, TTC17 localizes to the ER and interacts with a wide variety of chaperones and cochaperones normally associated with ER protein folding, quality control, and maturation processes. TTC17 was found to be significantly upregulated by ER stress and through the creation and use of TTC17

Identifiants

pubmed: 37949225
pii: S0021-9258(23)02478-X
doi: 10.1016/j.jbc.2023.105450
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

105450

Informations de copyright

Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.

Auteurs

Nathan P Canniff (NP)

Program in Molecular and Cellular Biology, University of Massachusetts Amherst, USA.

Jill B Graham (JB)

Program in Molecular and Cellular Biology, University of Massachusetts Amherst, USA.

Kevin P Guay (KP)

Program in Molecular and Cellular Biology, University of Massachusetts Amherst, USA.

Daniel A Lubicki (DA)

Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, USA.

Stephen J Eyles (SJ)

Program in Molecular and Cellular Biology, University of Massachusetts Amherst, USA; Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, USA; Institute for Applied Life Sciences, Mass Spectrometry Center, University of Massachusetts Amherst, USA.

Jennifer N Rauch (JN)

Program in Molecular and Cellular Biology, University of Massachusetts Amherst, USA; Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, USA.

Daniel N Hebert (DN)

Program in Molecular and Cellular Biology, University of Massachusetts Amherst, USA; Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, USA. Electronic address: dhebert@biochem.umass.edu.

Classifications MeSH