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Molecular basis for the recognition of steroidogenic acute regulatory protein by the 14‐3‐3 protein family
Author(s) -
Tugaeva Kristina V.,
Titterington James,
Sotnikov Dmitriy V.,
Maksimov Eugene G.,
Antson Alfred A.,
Sluchanko Nikolai N.
Publication year - 2020
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15474
Subject(s) - steroidogenic acute regulatory protein , mitochondrion , phosphorylation , cholesterol side chain cleavage enzyme , cleavage (geology) , biology , microbiology and biotechnology , chemistry , biochemistry , gene , paleontology , fracture (geology) , messenger rna
The human STARD1 protein supplies cholesterol to the mitochondria to initiate steroidogenesis. STARD1 functioning is regulated by binding to the 14‐3‐3 protein. We show that recognition by 14‐3‐3 is triggered by STARD1 phosphorylation at Ser57 and Ser195 by protein kinase A. Our observations are substantiated by biochemical evidence and crystal structures of 14‐3‐3 complexes with Ser57 and Ser195 phosphopeptides, revealing distinct roles for the two phosphosites in steroidogenesis regulation.