Everything you ever wanted to know about PKA regulation and its involvement in mammalian sperm capacitation

被引:39
作者
Baro Graf, Carolina [1 ,2 ]
Ritagliati, Carla [1 ]
Stival, Cintia [1 ]
Luque, Guillermina M. [3 ]
Gentile, Inaki [1 ]
Buffone, Mariano G. [3 ]
Krapf, Dario [1 ,2 ]
机构
[1] CONICET UNR, Lab Cell Signal Transduct Networks, Inst Biol Mol & Celular Rosario IBR, Rosario, Argentina
[2] Univ Nacl Rosario, Fac Ciencias Bioquim & Farrnaceut, Lab Med Reprod LMR, Rosario, Argentina
[3] Consejo Nacl Invest Cient & Tecn, Lab Cellular & Mol Reprod Biol, Inst Biol & Med Expt IBYME, Buenos Aires, DF, Argentina
关键词
Protein kinase A (PKA); Sperm capacitation; Reproduction; cAMP; PROTEIN-KINASE-A; SOLUBLE ADENYLYL-CYCLASE; EPSILON-N-ACETYLLYSINE; BOVINE CARDIAC-MUSCLE; CATALYTIC SUBUNIT; MOUSE SPERM; TYROSINE PHOSPHORYLATION; ANCHORING PROTEIN; FIBROUS SHEATH; LYSINE ACETYLATION;
D O I
10.1016/j.mce.2020.110992
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The 3', 5'-cyclic adenosine monophosphate (cAMP) dependent protein kinase (PKA) is a tetrameric holoenzyme comprising a set of two regulatory subunits (PKA-R) and two catalytic (PKA-C) subunits. The PKA-R subunits act as sensors of cAMP and allow PKA-C activity. One of the first signaling events observed during mammalian sperm capacitation is PKA activation. Thus, understanding how PKA activity is restricted in space and time is crucial to decipher the critical steps of sperm capacitation. It is widely accepted that PKA specificity depends on several levels of regulation. Anchoring proteins play a pivotal role in achieving proper localization signaling, subcellular targeting and cAMP microdomains. These multi-factorial regulation steps are necessary for a precise spatiotemporal activation of PKA. Here we discuss recent understanding of regulatory mechanisms of PKA in mammalian sperm, such as post-translational modifications, in the context of its role as the master orchestrator of molecular events conducive to capacitation.
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页数:18
相关论文
共 275 条
[81]   Engineering of a red-light-activated human cAMP/cGMP-specific phosphodiesterase [J].
Gasser, Carlos ;
Taiber, Sandra ;
Yeh, Chen-Min ;
Wittig, Charlotte Helene ;
Hegemann, Peter ;
Ryu, Soojin ;
Wunder, Frank ;
Moeglich, Andreas .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (24) :8803-8808
[82]   A role for SSeCKS, a major protein kinase C substrate with tumour suppressor activity, in cytoskeletal architecture, formation of migratory processes, and cell migration during embryogenesis [J].
Gelman, IH ;
Tombler, E ;
Vargas, J .
HISTOCHEMICAL JOURNAL, 2000, 32 (01) :13-26
[83]   Cloning and characterization of the human soluble adenylyl cyclase [J].
Geng, WD ;
Wang, ZG ;
Zhang, JN ;
Reed, BY ;
Pak, CYC ;
Moe, OW .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2005, 288 (06) :C1305-C1316
[84]   The cAMP/PKA Pathway Rapidly Activates SIRT1 to Promote Fatty Acid Oxidation Independently of Changes in NAD+ [J].
Gerhart-Hines, Zachary ;
Dominy, John E., Jr. ;
Blaettler, Sharon M. ;
Jedrychowski, Mark P. ;
Banks, Alexander S. ;
Lim, Ji-Hong ;
Chim, Helen ;
Gygi, Steven P. ;
Puigserver, Pere .
MOLECULAR CELL, 2011, 44 (06) :851-863
[85]  
GERSHEY EL, 1968, J BIOL CHEM, V243, P5018
[86]   IDENTIFICATION OF ELECTROSTATIC INTERACTIONS THAT DETERMINE THE PHOSPHORYLATION SITE SPECIFICITY OF THE CAMP-DEPENDENT PROTEIN-KINASE [J].
GIBBS, CS ;
ZOLLER, MJ .
BIOCHEMISTRY, 1991, 30 (22) :5329-5334
[87]   Acetylation and deacetylation of non-histone proteins [J].
Glozak, MA ;
Sengupta, N ;
Zhang, XH ;
Seto, E .
GENE, 2005, 363 :15-23
[88]  
GRANOT J, 1980, J BIOL CHEM, V255, P4569
[89]   Two novel brain-specific splice variants of the murine C beta gene of cAMP-dependent protein kinase [J].
Guthrie, CR ;
Skalhegg, BS ;
McKnight, GS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (47) :29560-29565
[90]   Role of the ionic environment and internal pH on sperm activity [J].
Hamamah, S ;
Gatti, JL .
HUMAN REPRODUCTION, 1998, 13 :20-30