Seeing your partner: Structural elucidation of the first C8 tetraspanin protein

Katrina J Binger; Mark D Wright

doi:10.1016/j.str.2022.01.003

Seeing your partner: Structural elucidation of the first C8 tetraspanin protein

Structure. 2022 Feb 3;30(2):203-205. doi: 10.1016/j.str.2022.01.003.

Authors

Katrina J Binger¹, Mark D Wright²

Affiliations

¹ Department of Biochemistry and Chemistry, La Trobe Institute for Molecular Sciences, La Trobe University, Bundoora, VIC 3086, Australia; Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3052, Australia; Department of Immunology and Pathology, Alfred Research Alliance, Central Clinical School, Monash University, Melbourne, VIC 3004, Australia.
² Department of Immunology and Pathology, Alfred Research Alliance, Central Clinical School, Monash University, Melbourne, VIC 3004, Australia. Electronic address: mark.wright@monash.edu.

PMID: 35120595
DOI: 10.1016/j.str.2022.01.003

Abstract

Tetraspanins are proteins that organize cell membranes via interactions with partner proteins mediated by their large ectodomain. In this issue of Structure, Lipper et al., 2022 have elucidated the structure of the first C8 tetraspanin and expand functional insight into how C8 tetraspanins regulate substrate specificity for the transmembrane protease ADAM10.

Publication types

Comment

MeSH terms

ADAM10 Protein / metabolism
Amyloid Precursor Protein Secretases* / chemistry
Amyloid Precursor Protein Secretases* / metabolism
Cell Membrane / metabolism
Membrane Proteins* / chemistry
Tetraspanins / chemistry
Tetraspanins / genetics
Tetraspanins / metabolism

Substances

Membrane Proteins
Tetraspanins
Amyloid Precursor Protein Secretases
ADAM10 Protein