Huntingtin-associated Protein 1 (HAP1) Is a cGMP-dependent Kinase Anchoring Protein (GKAP) Specific for the cGMP-dependent Protein Kinase Iβ Isoform

Corradini, Eleonora; Burgers, Pepijn P.; Plank, Michaël; Heck, Albert J. R.; Scholten, Arjen

doi:10.1074/jbc.m114.622613

Cited by 14 publications

(4 citation statements)

References 48 publications

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“…The presence of cGMP-interacting proteins can be studied using, for example, proteomics, and previous such investigations have indeed resulted in the discovery of such proteins in multiple tissues (Kim & Park, 2003;Scholten et al, 2006Scholten et al, , 2007. Regular cG-MP-interacting proteins include PKG (Corradini et al, 2015;Francis et al, 2005;Francis & Corbin, 2013;Paquet-Durand et al, 2009), and cAMP-dependent protein kinase (PKA), which shares homology with PKG (Francis & Corbin, 2013) and which can be cross-activated by cGMP, as well as CNG-channels, phosphodiesterases, and cGMP transport proteins (Francis et al, 2005). However, seemingly unrelated proteins have also been reported as potential interactors, like the mitogen-activated protein kinase I (MAPKI) (Kim & Park, 2003).…”

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confidence: 99%

The cGMP system in normal and degenerating mouse neuroretina: New proteins with cGMP interaction potential identified by a proteomics approach

Rasmussen

Welinder

Schwede

et al. 2020

Journal of Neurochemistry

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The hereditary disease Retinitis pigmentosa results in severe vision loss due to photoreceptor degeneration by unclear mechanisms. In several disease models, the second messenger cGMP accumulates in the degenerating photoreceptors, where it may over‐activate specific cGMP‐interacting proteins, like cGMP‐dependent protein kinase. Moreover, interventions that counteract the activity of these proteins lead to reduced photoreceptor cell death. Yet there is little or no information whether other than such regular cGMP‐interactors are present in the retina, which we, therefore, investigated in wild‐type and retinal degeneration (rd1, rd10, and rd2) mouse models. An affinity chromatography based proteomics approach that utilized immobilized cGMP analogs was applied to enrich and select for regular and potentially new cGMP‐interacting proteins as identified by mass spectrometry. This approach revealed 12 regular and 10 potentially new retinal cGMP‐interacting proteins (e.g., EPAC2 and CaMKIIα). Several of the latter were found to be expressed in the photoreceptors and to have proximity to cGMP and may thus be of interest when defining prospective therapeutic targets or biomarkers for retinal degeneration.

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confidence: 99%

The cGMP system in normal and degenerating mouse neuroretina: New proteins with cGMP interaction potential identified by a proteomics approach

Rasmussen

Welinder

Schwede

et al. 2020

Journal of Neurochemistry

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“…Similarly, cyclic GMP can activate CNG ion channels [ 13 ], can act on alternate non-canonical kinases besides PKG and can have kinase-independent effects as well [ 9 ]. Cyclic nucleotide signaling can be largely governed by internal localization via scaffolding proteins such as A-kinase anchoring protein for cyclic AMP [ 18 ] and inositol 1,4,5-triphosphate (IP 3 ) receptor-associated cGMP kinase substrate (IRAG) and Huntingtin-associated protein 1 (HAP1) for cyclic GMP [ 19 , 20 ]. Lastly, persistence of cyclic AMP and cyclic GMP signals is largely governed by specific phosphodiesterases (PDEs), which cleave their phosphodiester bonds and degrade them into inactive 5′-monophosphates [ 21 ].…”

Section: Cyclic Nucleotides and Cyclic Nucleotide-directed Proteinmentioning

confidence: 99%

Cyclic Nucleotide-Directed Protein Kinases in Cardiovascular Inflammation and Growth

Holland

Francisco

Johnson

et al. 2018

JCDD

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Cardiovascular disease (CVD), including myocardial infarction (MI) and peripheral or coronary artery disease (PAD, CAD), remains the number one killer of individuals in the United States and worldwide, accounting for nearly 18 million (>30%) global deaths annually. Despite considerable basic science and clinical investigation aimed at identifying key etiologic components of and potential therapeutic targets for CVD, the number of individuals afflicted with these dreaded diseases continues to rise. Of the many biochemical, molecular, and cellular elements and processes characterized to date that have potential to control foundational facets of CVD, the multifaceted cyclic nucleotide pathways continue to be of primary basic science and clinical interest. Cyclic adenosine monophosphate (cyclic AMP) and cyclic guanosine monophosphate (cyclic GMP) and their plethora of downstream protein kinase effectors serve ubiquitous roles not only in cardiovascular homeostasis but also in the pathogenesis of CVD. Already a major target for clinical pharmacotherapy for CVD as well as other pathologies, novel and potentially clinically appealing actions of cyclic nucleotides and their downstream targets are still being discovered. With this in mind, this review article focuses on our current state of knowledge of the cyclic nucleotide-driven serine (Ser)/threonine (Thr) protein kinases in CVD with particular emphasis on cyclic AMP-dependent protein kinase (PKA) and cyclic GMP-dependent protein kinase (PKG). Attention is given to the regulatory interactions of these kinases with inflammatory components including interleukin 6 signals, with G protein-coupled receptor and growth factor signals, and with growth and synthetic transcriptional platforms underlying CVD pathogenesis. This article concludes with a brief discussion of potential future directions and highlights the importance for continued basic science and clinical study of cyclic nucleotide-directed protein kinases as emerging and crucial controllers of cardiac and vascular disease pathologies.

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“…PKs that share high sequence similarity can be confined to different intracellular compartments by their interaction partners: for example, while Aurora A resides at the centrosome and spindle microtubules by virtue of interaction with proteins Ajuba and TPX2 [9], Aurora B is enriched at the centromeric region of chromosomes by forming complex with proteins INCENP, Survivin, and Borealin [10]. Even PKs that reside in cytosol are frequently targeted to a certain cellular location by a scaffolding protein; for example, Ca 2+ -activated PKs are located in the vicinity of Ca 2+ -channels on the plasma membrane or endoplasmic reticulum, while cAMP-dependent PKs are located in the vicinity of adenylyl cyclase [11][12][13]. The same scaffolding protein that is responsible for localization of a PK might also offer binding sites for its substrates, but also protein phosphatases and enzymes that degrade secondary messengers (e.g., phosphodiesterases).…”

Section: Brief Insight Into Structure and Function Of Protein Kinasesmentioning

confidence: 99%

Dissection of Protein Kinase Pathways in Live Cells Using Photoluminescent Probes: Surveillance or Interrogation?

2018

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Protein kinases catalyze phosphorylation, a small yet crucial modification that affects participation of the substrate proteins in the intracellular signaling pathways. The activity of 538 protein kinases encoded in human genome relies upon spatiotemporally controlled mechanisms, ensuring correct progression of virtually all physiological processes on the cellular level-from cell division to cell death. The aberrant functioning of protein kinases is linked to a wide spectrum of major health issues including cancer, cardiovascular diseases, neurodegenerative diseases, inflammatory diseases, etc. Hence, significant effort of scientific community has been dedicated to the dissection of protein kinase pathways in their natural milieu. The combination of recent advances in the field of light microscopy, the wide variety of genetically encoded or synthetic photoluminescent scaffolds, and the techniques for intracellular delivery of cargoes has enabled design of a plethora of probes that can report activation of target protein kinases in human live cells. The question remains: how much do we bias intracellular signaling of protein kinases by monitoring it? This review seeks answers to this question by analyzing different classes of probes according to their general structure, mechanism of recognition of biological target, and optical properties necessary for the reporting of intracellular events.

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Huntingtin-associated Protein 1 (HAP1) Is a cGMP-dependent Kinase Anchoring Protein (GKAP) Specific for the cGMP-dependent Protein Kinase Iβ Isoform

Cited by 14 publications

References 48 publications

The cGMP system in normal and degenerating mouse neuroretina: New proteins with cGMP interaction potential identified by a proteomics approach

The cGMP system in normal and degenerating mouse neuroretina: New proteins with cGMP interaction potential identified by a proteomics approach

Cyclic Nucleotide-Directed Protein Kinases in Cardiovascular Inflammation and Growth

Dissection of Protein Kinase Pathways in Live Cells Using Photoluminescent Probes: Surveillance or Interrogation?

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