A new role for 14-3-3 protein in steroidogenesis

. 2020 Sep ; 287 (18) : 3921-3924. [epub] 20200816

Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic

Typ dokumentu časopisecké články, práce podpořená grantem, komentáře

Perzistentní odkaz   https://www.medvik.cz/link/pmid32852115

Steroidogenic acute regulatory protein (STARD1) is regulated by phosphorylation and 14-3-3 protein binding. STARD1 is a key player in cholesterol transport in mitochondria, and its regulation is not fully understood. Tugaeva et al. provide novel insights on the site-specific phosphorylation and subsequent 14-3-3-dependent regulation of STARD1 function. These results may help us understand the mechanism behind the regulation of steroidogenesis. Comment on: https://doi.org/10.1111/febs.15474.

Komentář

PubMed

Zobrazit více v PubMed

Cohen P (2002) The origins of protein phosphorylation. Nat Cell Biol 4, E127-E130.

Sluchanko NN (2018) Association of multiple phosphorylated proteins with the 14-3-3 regulatory hubs: problems and perspectives. J Mol Biol 430, 20-26.

Obsil T, Ghirlando R, Klein DC, Ganguly S & Dyda F (2001) Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation. Cell 105, 257-267.

Ottmann C, Marco S, Jaspert N, Marcon C, Schauer N, Weyand M, Vandermeeren C, Duby G, Boutry M, Wittinghofer A et al. (2007) Structure of a 14-3-3 coordinated hexamer of the plant plasma membrane H+ -ATPase by combining X-ray crystallography and electron cryomicroscopy. Mol Cell 25, 427-440.

Taoka K, Ohki I, Tsuji H, Furuita K, Hayashi K, Yanase T, Yamaguchi M, Nakashima C, Purwestri YA, Tamaki S et al. (2011) 14-3-3 proteins act as intracellular receptors for rice Hd3a florigen. Nature 476, 332-335.

Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB & Strelkov SV (2017) Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator. Structure 25, 305-316.

Alblova M, Smidova A, Docekal V, Vesely J, Herman P, Obsilova V & Obsil T (2017) Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1. Proc Natl Acad Sci USA 114, E9811-E9820.

Karlberg T, Hornyak P, Pinto AF, Milanova S, Ebrahimi M, Lindberg M, Pullen N, Nordstrom A, Loverli E, Caraballo R et al. (2018) 14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface. Nat Commun 9, 3785.

Kondo Y, Ognjenovic J, Banerjee S, Karandur D, Merk A, Kulhanek K, Wong K, Roose JP, Subramaniam S & Kuriyan J (2019) Cryo-EM structure of a dimeric B-Raf:14-3-3 complex reveals asymmetry in the active sites of B-Raf kinases. Science 366, 109-115.

Park E, Rawson S, Li K, Kim BW, Ficarro SB, Pino GG, Sharif H, Marto JA, Jeon H & Eck MJ (2019) Architecture of autoinhibited and active BRAF-MEK1-14-3-3 complexes. Nature 575, 545-550.

Tugaeva KV, Titterington J, Sotnikov DV, Maksimov EG, Antson AA & Sluchanko NN (2020) Molecular basis for the recognition of steroidogenic acute regulatory protein by the 14-3-3 protein family. FEBS J. 3944-3966.

Tugaeva KV & Sluchanko NN (2019) Steroidogenic acute regulatory protein: structure, functioning, and regulation. Biochemistry (Mosc) 84, S233-S253.

Tsujishita Y & Hurley JH (2000) Structure and lipid transport mechanism of a StAR-related domain. Nat Struct Biol 7, 408-414.

Bose HS, Whittal RM, Baldwin MA & Miller WL (1999) The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule. Proc Natl Acad Sci USA 96, 7250-7255.

Arakane F, King SR, Du Y, Kallen CB, Walsh LP, Watari H, Stocco DM & Strauss JF 3rd (1997) Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity. J Biol Chem 272, 32656-32662.

Aghazadeh Y, Rone MB, Blonder J, Ye X, Veenstra TD, Hales DB, Culty M & Papadopoulos V (2012) Hormone-induced 14-3-3gamma adaptor protein regulates steroidogenic acute regulatory protein activity and steroid biosynthesis in MA-10 Leydig cells. J Biol Chem 287, 15380-15394.

Najít záznam

Citační ukazatele

Pouze přihlášení uživatelé

Možnosti archivace

Nahrávání dat ...