Cancer associated mutations in Sec61γ alter the permeability of the ER translocase

Translocation of secretory and integral membrane proteins across or into the ER membrane occurs via the Sec61 complex, a heterotrimeric protein complex possessing two essential sub-units, Sec61p/Sec61a and Sss1p/Sec61γ and the non-essential Sbh1p/Sec61β subunit. In addition to forming a protein cond...

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Main Authors: Witham, Christopher M., Paxman, Aleshanee L., Baklous, Lamprini, Steuart, Robert F.L., Schulz, B.L., Mousley, Carl J.
Format: Journal Article
Language:English
Published: PUBLIC LIBRARY SCIENCE 2021
Subjects:
Online Access:http://hdl.handle.net/20.500.11937/96048
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author Witham, Christopher M.
Paxman, Aleshanee L.
Baklous, Lamprini
Steuart, Robert F.L.
Schulz, B.L.
Mousley, Carl J.
author_facet Witham, Christopher M.
Paxman, Aleshanee L.
Baklous, Lamprini
Steuart, Robert F.L.
Schulz, B.L.
Mousley, Carl J.
author_sort Witham, Christopher M.
building Curtin Institutional Repository
collection Online Access
description Translocation of secretory and integral membrane proteins across or into the ER membrane occurs via the Sec61 complex, a heterotrimeric protein complex possessing two essential sub-units, Sec61p/Sec61a and Sss1p/Sec61γ and the non-essential Sbh1p/Sec61β subunit. In addition to forming a protein conducting channel, the Sec61 complex maintains the ER permeability barrier, preventing flow of molecules and ions. Loss of Sec61 integrity is detrimental and implicated in the progression of disease. The Sss1p/Sec61? C-terminus is juxtaposed to the key gating module of Sec61p/Sec61a and is important for gating the translocon. Inspection of the cancer genome database identifies six mutations in highly conserved amino acids of Sec61γ/Sss1p. We identify that five out of the six mutations identified affect gating of the ER translocon, albeit with varying strength. Together, we find that mutations in Sec61γ that arise in malignant cells result in altered translocon gating dynamics, this offers the potential for the translocon to represent a target in co-therapy for cancer treatment.
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spelling curtin-20.500.11937-960482024-11-13T07:19:23Z Cancer associated mutations in Sec61γ alter the permeability of the ER translocase Witham, Christopher M. Paxman, Aleshanee L. Baklous, Lamprini Steuart, Robert F.L. Schulz, B.L. Mousley, Carl J. Science & Technology Life Sciences & Biomedicine Genetics & Heredity SIGNAL RECOGNITION PROTEIN ENDOPLASMIC-RETICULUM MEMBRANE-PROTEIN BOUND RIBOSOMES CROSS-LINKING CA2+ YEAST PEPTIDE CHANNEL SSS1P Amino Acid Sequence Biological Transport Cell Membrane Permeability Endoplasmic Reticulum Membrane Proteins Membrane Transport Proteins Mutation Neoplasms Protein Transport SEC Translocation Channels Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Endoplasmic Reticulum Saccharomyces cerevisiae Neoplasms Membrane Transport Proteins Saccharomyces cerevisiae Proteins Membrane Proteins Cell Membrane Permeability Amino Acid Sequence Biological Transport Protein Transport Mutation SEC Translocation Channels Translocation of secretory and integral membrane proteins across or into the ER membrane occurs via the Sec61 complex, a heterotrimeric protein complex possessing two essential sub-units, Sec61p/Sec61a and Sss1p/Sec61γ and the non-essential Sbh1p/Sec61β subunit. In addition to forming a protein conducting channel, the Sec61 complex maintains the ER permeability barrier, preventing flow of molecules and ions. Loss of Sec61 integrity is detrimental and implicated in the progression of disease. The Sss1p/Sec61? C-terminus is juxtaposed to the key gating module of Sec61p/Sec61a and is important for gating the translocon. Inspection of the cancer genome database identifies six mutations in highly conserved amino acids of Sec61γ/Sss1p. We identify that five out of the six mutations identified affect gating of the ER translocon, albeit with varying strength. Together, we find that mutations in Sec61γ that arise in malignant cells result in altered translocon gating dynamics, this offers the potential for the translocon to represent a target in co-therapy for cancer treatment. 2021 Journal Article http://hdl.handle.net/20.500.11937/96048 10.1371/journal.pgen.1009780 English http://creativecommons.org/licenses/by/4.0/ PUBLIC LIBRARY SCIENCE fulltext
spellingShingle Science & Technology
Life Sciences & Biomedicine
Genetics & Heredity
SIGNAL RECOGNITION PROTEIN
ENDOPLASMIC-RETICULUM
MEMBRANE-PROTEIN
BOUND RIBOSOMES
CROSS-LINKING
CA2+
YEAST
PEPTIDE
CHANNEL
SSS1P
Amino Acid Sequence
Biological Transport
Cell Membrane Permeability
Endoplasmic Reticulum
Membrane Proteins
Membrane Transport Proteins
Mutation
Neoplasms
Protein Transport
SEC Translocation Channels
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Endoplasmic Reticulum
Saccharomyces cerevisiae
Neoplasms
Membrane Transport Proteins
Saccharomyces cerevisiae Proteins
Membrane Proteins
Cell Membrane Permeability
Amino Acid Sequence
Biological Transport
Protein Transport
Mutation
SEC Translocation Channels
Witham, Christopher M.
Paxman, Aleshanee L.
Baklous, Lamprini
Steuart, Robert F.L.
Schulz, B.L.
Mousley, Carl J.
Cancer associated mutations in Sec61γ alter the permeability of the ER translocase
title Cancer associated mutations in Sec61γ alter the permeability of the ER translocase
title_full Cancer associated mutations in Sec61γ alter the permeability of the ER translocase
title_fullStr Cancer associated mutations in Sec61γ alter the permeability of the ER translocase
title_full_unstemmed Cancer associated mutations in Sec61γ alter the permeability of the ER translocase
title_short Cancer associated mutations in Sec61γ alter the permeability of the ER translocase
title_sort cancer associated mutations in sec61γ alter the permeability of the er translocase
topic Science & Technology
Life Sciences & Biomedicine
Genetics & Heredity
SIGNAL RECOGNITION PROTEIN
ENDOPLASMIC-RETICULUM
MEMBRANE-PROTEIN
BOUND RIBOSOMES
CROSS-LINKING
CA2+
YEAST
PEPTIDE
CHANNEL
SSS1P
Amino Acid Sequence
Biological Transport
Cell Membrane Permeability
Endoplasmic Reticulum
Membrane Proteins
Membrane Transport Proteins
Mutation
Neoplasms
Protein Transport
SEC Translocation Channels
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Endoplasmic Reticulum
Saccharomyces cerevisiae
Neoplasms
Membrane Transport Proteins
Saccharomyces cerevisiae Proteins
Membrane Proteins
Cell Membrane Permeability
Amino Acid Sequence
Biological Transport
Protein Transport
Mutation
SEC Translocation Channels
url http://hdl.handle.net/20.500.11937/96048