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Proteasome complexes experience profound structural and functional rearrangements throughout mammalian spermatogenesis
Author(s) -
Dušan Živković,
Angelique Sanchez Dafun,
Thomas Menneteau,
Adrien Schahl,
Sandrine Lise,
Christine Kervarrec,
Ana Toste Rêgo,
Paula C. A. da Fonseca,
Matthieu Chavent,
Charles Pineau,
Odile BurletSchiltz,
Julien Marcoux,
MariePierre Bousquet
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2116826119
Subject(s) - biology , proteasome , microbiology and biotechnology , meiosis , germ cell , population , protein subunit , spermatogenesis , genetics , gene , sociology , demography , endocrinology
Significance The proteasome is responsible for the homeostasis of intracellular proteins. Here, we describe structural and functional aspects of a poorly characterized proteasome subtype found exclusively in germ cells. The spermatoproteasome was recently shown to be essential for spermatogenesis, a process requiring intense proteolysis. It differs from the constitutive proteasome by only one subunit, α4s, a subunit that replaces its α4 ubiquitous counterpart. In this work, we show how the shift from α4 to α4s regulates proteasome composition, dynamics, interactome, and activity. We reveal a regulation process more complex than previously suggested, which provides the basis for structural and functional studies of the spermatoproteasome.

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