AKAP3 Selectively Binds PDE4A Isoforms in Bovine Spermatozoa1

Bajpai, Malini; Fiedler, Sarah E.; Huang, Zaohua; Vijayaraghavan, Srinivasan; Olson, Gary E.; Livera, Gabriel; Conti, Marco; Carr, Daniel W.

doi:10.1095/biolreprod.105.043588

Cited by 63 publications

(59 citation statements)

References 56 publications

(67 reference statements)

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“…See Tasken and Aandahl [27] the protein phosphatases PP1 and PP2A (Figure 1b). Likewise, AKAP110 targets the PDE4A isoform to the acrosome of sperm, whereas AKAP149 and AKAP121 and the Nervy and myeloid translocation gene (MTG) anchoring proteins, respectively, target the PDE4A and PDE7A isoforms to various subcellular locations [46,47] (Figure 1c). These AKAP-PKA-PDE units respond to upstream signals that emanate from GPCR and adenylyl cyclase networks, creating a complex and continually changing signaling environment in which cAMP concentrations are distributed unevenly in the cell.…”

Section: Akaps and Phosphodiesterases: Compartmentalization Of Camp Amentioning

confidence: 99%

The where's and when's of kinase anchoring

Smith

Langeberg

Scott

2006

Trends in Biochemical Sciences

130

132

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Kinase anchoring has gained acceptance as a means to synchronize spatial and temporal aspects of cell signaling. A-kinase anchoring proteins (AKAPs) are a diverse group of functionally related proteins that target protein kinase A and other enzymes to coordinate a range of signaling events. Recent advances in this field have shown that incorporating phosphodiesterases into AKAP signaling complexes exerts local control of cAMP metabolism, that phosphorylation of some AKAPs potentiates downstream signaling events, that anchoring of distinct enzyme combinations functions as a mechanism to expand the repertoire of cellular events controlled by a single AKAP, and that fluorescent biosensors can be used to visualize dynamic aspects of localized cAMP signaling. IntroductionA half-century of work has proclaimed protein phosphorylation as a principal means of reversibly controlling biochemical events. It began when Fischer and Krebs [1] demonstrated that conversion of inactive muscle phosphorylase b into active phosphorylase a requires ATP and is catalyzed by a phosphorylase b kinase. They then showed that phosphorylase b kinase itself is controlled by a serine kinase that is responsive to the second messenger cAMP. Together with their colleagues, they subsequently discovered protein kinase A (PKA) and the concept of a 'kinase cascade' [2].From these humble beginnings the field of protein kinase research was born, paving the way for the discovery of phosphotyrosine by Hunter and co-workers [3], the identification of Src tyrosine kinase by Brugge and Ericsson et al. [4], the seminal work of Pawson and associates on phosphotyrosine recognition motifs [5], and the resolution of a crystal structure of the PKA catalytic subunit by Taylor and colleagues [6]. Consequently, we now recognize that the w518 members of the human kinome represent a superfamily of enzymes that participate in all aspects of cellular regulation [7].Protein kinase research is now focusing on how these enzymes are organized in relation to their effectors and substrates within the three dimensions of the cell. Interestingly, the study of PKA is shedding new light on the complexity of these protein-protein interactions.

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Section: Akaps and Phosphodiesterases: Compartmentalization Of Camp Amentioning

confidence: 99%

The where's and when's of kinase anchoring

Smith

Langeberg

Scott

2006

Trends in Biochemical Sciences

130

132

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“…Both AKAP3 and AKAP4 are present in the fibrous sheath of the sperm flagellum, control PKA activity and undergo phosphorylation during the capacitation process [83][84][85]. AKAP complexes also modulate the motility of sperm.…”

Section: Function Of S-nitrosoproteins In Spermatozoamentioning

confidence: 99%

Nitric Oxide: Key Features in Spermatozoa

Staicu¹,

Parra²

2017

Nitric Oxide Synthase - Simple Enzyme-Complex Roles

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Several in vitro studies have pointed to the importance of nitric oxide (NO) in the female and male reproductive system in mammals. Its functions vary from preventing oocyte aging, improving the integrity of the microtubular spindle apparatus in aged oocytes, modulating the contraction of the oviduct, to regulating sperm physiology by affecting the motility, inducing chemotaxis in spermatozoa, regulating tyrosine phosphorylation, enhancing the sperm-zona pellucida binding ability, and modulating the acrosomal reaction. In spermatozoa, NO exerts its functions in different ways, which involve key elements such as the soluble isoform of guanylate cyclase, cyclic guanosine monophosphate (cGMP), cyclic adenosine monophosphate (cAMP), protein kinase A (PKA), adenylate cyclase, and the extracellular signal-regulated kinase (ERK) pathway. Furthermore, NO leads to the S-nitrosylation of several sperm proteins, among them a substantial group associated with energy generation and cell movement, but also with signal transduction, suggesting a role for S-nitrosylation in sperm motility and in modulating the sperm function, respectively. In this chapter, an overview of how NO modulates the sperm physiology is presented, based on the knowledge acquired to this day.

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“…PDE4A4/5 is expressed in a wide variety of tissues, including the pituitary (Mackenzie et al 2008, Lennox et al 2011, and both membrane and cytosolic localisation has been detected (Huston et al 2000). PDE4A5 was demonstrated to interact with the SH3 domains of SRC family tyrosyl kinases (O'Connell et al 1996, Beard et al 2002, with AKAP3 (Bajpai et al 2006) and with AIP (Bolger et al 2003). AIP was initially identified as a direct binding partner of PDE4A5 by a Y2H screening of a rat brain cDNA library.…”

Section: Pde4a5mentioning

confidence: 99%

AIP and its interacting partners

Trivellin¹,

Korbonits²

2011

Journal of Endocrinology

130

119

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Germline mutations in the aryl hydrocarbon receptorinteracting protein gene (AIP) predispose to young-onset pituitary tumours, most often to GH-or prolactin-secreting adenomas, and most of these patients belong to familial isolated pituitary adenoma families. The molecular pathway initiated by the loss-of-function AIP mutations leading to pituitary tumour formation is unknown. AIP, a co-chaperone of heat-shock protein 90 and various nuclear receptors, belongs to the family of tetratricopeptide repeat (TPR)-containing proteins. It has three antiparallel a-helix motifs (TPR domains) that mediate the interaction of AIP with most of its partners. In this review, we summarise the known interactions of AIP described so far. The identification of AIP partners and the understanding of how AIP interacts with these proteins might help to explain the specific phenotype of the families with heterozygous AIP mutations, to gain deeper insight into the pathological process of pituitary tumour formation and to identify novel drug targets.

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AKAP3 Selectively Binds PDE4A Isoforms in Bovine Spermatozoa1

Cited by 63 publications

References 56 publications

The where's and when's of kinase anchoring

The where's and when's of kinase anchoring

Nitric Oxide: Key Features in Spermatozoa

AIP and its interacting partners

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