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Article|Online Now
Structure of the human signal peptidase complex reveals the determinants for
signal peptide cleavage
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STRUCTURE OF THE HUMAN SIGNAL PEPTIDASE COMPLEX REVEALS THE DETERMINANTS FOR
SIGNAL PEPTIDE CLEAVAGE
* A. Manuel Liaci
A. Manuel Liaci
Affiliations
Structural Biochemistry, Bijvoet Centre for Biomolecular Research, Utrecht
University, Universiteitsweg 99, 3584 CG, Utrecht, the Netherlands
Search for articles by this author
* Barbara Steigenberger 7
Author Footnotes
7 These authors contributed equally
Barbara Steigenberger
Footnotes
7 These authors contributed equally
Affiliations
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for
Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences,
Utrecht University, Padualaan 8, 3584 CH, Utrecht, the Netherlands
Netherlands Proteomics Centre, Padualaan 8, 3584 CH, Utrecht, the Netherlands
Search for articles by this author
* Paulo Cesar Telles de Souza 7
Author Footnotes
7 These authors contributed equally
Paulo Cesar Telles de Souza
Footnotes
7 These authors contributed equally
Affiliations
Groningen Biomolecular Sciences and Biotechnology Institute and Zernike
Institute for Advanced Material, University of Groningen, Nijenborgh 7, 9747
AG, Groningen, the Netherlands
Molecular Microbiology and Structural Biochemistry, UMR 5086, CNRS and
University of Lyon, Lyon, France
Search for articles by this author
* Sem Tamara
Sem Tamara
Affiliations
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for
Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences,
Utrecht University, Padualaan 8, 3584 CH, Utrecht, the Netherlands
Netherlands Proteomics Centre, Padualaan 8, 3584 CH, Utrecht, the Netherlands
Search for articles by this author
* Mariska Gröllers-Mulderij
Mariska Gröllers-Mulderij
Affiliations
Structural Biochemistry, Bijvoet Centre for Biomolecular Research, Utrecht
University, Universiteitsweg 99, 3584 CG, Utrecht, the Netherlands
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* Patrick Ogrissek
Patrick Ogrissek
Affiliations
Structural Biochemistry, Bijvoet Centre for Biomolecular Research, Utrecht
University, Universiteitsweg 99, 3584 CG, Utrecht, the Netherlands
Institute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger
Allee 160, 23562 Lübeck, Germany
Search for articles by this author
*
* Siewert J. Marrink
Siewert J. Marrink
Affiliations
Groningen Biomolecular Sciences and Biotechnology Institute and Zernike
Institute for Advanced Material, University of Groningen, Nijenborgh 7, 9747
AG, Groningen, the Netherlands
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* Richard A. Scheltema
Richard A. Scheltema
Affiliations
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for
Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences,
Utrecht University, Padualaan 8, 3584 CH, Utrecht, the Netherlands
Netherlands Proteomics Centre, Padualaan 8, 3584 CH, Utrecht, the Netherlands
Search for articles by this author
* Friedrich Förster 8
Author Footnotes
8 Lead contact
Friedrich Förster
Correspondence
Corresponding author
Contact
Footnotes
8 Lead contact
Affiliations
Structural Biochemistry, Bijvoet Centre for Biomolecular Research, Utrecht
University, Universiteitsweg 99, 3584 CG, Utrecht, the Netherlands
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* Show all authors
* Show footnotesHide footnotes
Author Footnotes
7 These authors contributed equally
8 Lead contact
Published:August 12, 2021DOI:https://doi.org/10.1016/j.molcel.2021.07.031
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* Highlights
* Summary
* Graphical abstract
* Keywords
* References
* Article Info
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* Comments
HIGHLIGHTS
* •
The human SPC has two paralogs, both of which are structurally characterized
here
* •
The SPC is a serine protease with a catalytic Ser-His-Asp triad
* •
The c-region binding pocket is conserved to bacterial signal peptidases
* •
Membrane thinning by the SPC measures signal peptides for length before
cleavage
SUMMARY
The signal peptidase complex (SPC) is an essential membrane complex in the
endoplasmic reticulum (ER), where it removes signal peptides (SPs) from a large
variety of secretory pre-proteins with exquisite specificity. Although the
determinants of this process have been established empirically, the molecular
details of SP recognition and removal remain elusive. Here, we show that the
human SPC exists in two functional paralogs with distinct proteolytic subunits.
We determined the atomic structures of both paralogs using electron
cryo-microscopy and structural proteomics. The active site is formed by a
catalytic triad and abuts the ER membrane, where a transmembrane window
collectively formed by all subunits locally thins the bilayer. Molecular
dynamics simulations indicate that this unique architecture generates
specificity for SPs based on the length of their hydrophobic segments.
GRAPHICAL ABSTRACT
Graphical Abstract
* View Large Image
* Figure Viewer
* Download Hi-res image
KEYWORDS
* signal peptidase complex
* signal peptide
* protein maturation
* protein secretion
* ER translocon
* membrane thinning
* cryo-EM
* crosslinking mass spectrometry
* molecular dynamics simulations
* secretory pathway
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ARTICLE INFO
PUBLICATION HISTORY
Published: August 12, 2021
Accepted: July 26, 2021
Received in revised form: June 2, 2021
Received: December 1, 2020
PUBLICATION STAGE
In Press, Corrected Proof
IDENTIFICATION
DOI: https://doi.org/10.1016/j.molcel.2021.07.031
COPYRIGHT
© 2021 Elsevier Inc.
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Structure of the human signal peptidase complex reveals the determinants for
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