Phosducin and βγ-Transducin Interaction I: Effects of Post-translational Modifications

Chen, Fayu; Lee, Rehwa H.

doi:10.1006/bbrc.1997.6460

Cited by 28 publications

(20 citation statements)

References 27 publications

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“…The efficacy of Phd binding to G␤␥ is determined, in part, by its phosphorylation state at serine 73 (29). The balance between phosphorylation by cyclic AMP-dependent protein kinase A and dephosphorylation by protein phosphatase 2A results in an increase of phosphorylated Phd during darkness and its decrease upon exposure to light (4,9,25,26,29,63,65). The dephosphorylated form of Phd favors the binding of G␤␥, which, in light, prevents receptor-mediated G␣ reactivation (32,65) and blocks interactions between G␤␥ and its effectors (25,26,41,64).…”

mentioning

confidence: 99%

Modulation of CRX Transactivation Activity by Phosducin Isoforms

Zhu

Craft

2000

Molecular and Cellular Biology

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mentioning

confidence: 99%

Modulation of CRX Transactivation Activity by Phosducin Isoforms

Zhu

Craft

2000

Molecular and Cellular Biology

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“…An unexpected observation in these experiments was the reduced electrophoretic mobility displayed by G␤␥ extracted from light-stimulated ciliates. In vertebrate photoreceptor cells, the translocation of G␤␥ to the cytoplasm as a result of light stimulation has been reported, although a simultaneous shift in gel mobility was not observed (Yamamoto et al, 2007;Chen and Lee, 1997;Sokolov et al, 2004). Fig.·2 shows that the pool of G␤ localized in the ciliate cytoplasmic fraction was represented by a 36-kDa polypeptide (see control bovine rod outer segment preparation in Fig.·2, lane 7); in contrast, membrane-bound G␤ migrated on SDS-PAGE as a 32·kDa protein.…”

Section: Discussionmentioning

confidence: 94%

Phosducin interacts with the G-protein βγ-dimer of ciliate protozoanBlepharisma japonicumupon illumination

Sobierajska

Fabczak

2007

Journal of Experimental Biology

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SUMMARY Immunological techniques and high-resolution FRET analysis were employed to investigate the in vivo colocalization and interaction of phosducin(Pdc) with the βγ-subunits of G-protein (Gβγ) in the ciliate Blepharisma japonicum. Immunological techniques revealed that illumination of cells resulted in a decrease in phosphorylation levels of Pdc and its colocalization with Gβγ. The observed light-induced Pdc dephosphorylation was also accompanied by significant enhancement of Gβγ binding by this molecule. Possible formation of the Pdc–Gβγ complex in cells exposed to light was corroborated by FRET between these proteins. Treatment of cells with okadaic acid, an inhibitor of phosphatase activity, entirely prevented Pdc dephosphorylation by light, colocalization of this phosphoprotein with Gβγ and generation of the Pdc–Gβγ complex. Cell fractionation and immunoblotting revealed that in cells exposed to light, the formation of Pdc–Gβγ complex and its translocation into the cytoplasm occur simultaneously with a change in the gel migration of Gβ. Moreover, a 33 kDa immunoanalog of 14-3-3 protein was identified and we showed that this protein is bound by phosphorylated Pdc in a cell adapted to darkness. The results of this study provide additional detailed characterization of the functional properties of the ciliate Pdc. The likely functional role of Pdc in Blepharisma is discussed.

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“…/calmodulindependent protein kinase II (CaMKII) is able to phosphorylate phosducin within consensus phosphorylation sequences at Ser-73 or Ser-54. More recent publications have identified additional phosphorylation sites within the phosducin molecule and provided a more detailed view of phosphorylation/dephosphorylation kinetics and the degree of phosphorylation-induced functional inhibition [45,[55][56][57]. Accordingly, phosphorylation by PKA at Ser-73 was shown to diminish binding affinity of phosducin for G t bc by only threefold [43,53,55].…”

Section: Posttranslational Modificationmentioning

confidence: 99%

The physiological roles of phosducin: from retinal function to stress-dependent hypertension

Beetz

Hein

2010

Cell. Mol. Life Sci.

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In the time since its discovery, phosducin's functions have been intensively studied both in vivo and in vitro. Phosducin's most important biochemical feature in in vitro studies is its binding to heterotrimeric G protein βγ-subunits. Data on phosducin's in vivo relevance, however, have only recently been published but expand the range of biological actions, as shown both in animal models as well as in human studies. This review gives an overview of different aspects of phosducin biology ranging from structure, phylogeny of phosducin family members, posttranscriptional modification, biochemical features, localization and levels of expression to its physiological functions. Special emphasis will be placed on phosducin's function in the regulation of blood pressure. In the second part of this article, findings concerning cardiovascular regulation and their clinical relevance will be discussed on the basis of recently published data from gene-targeted mouse models and human genetic studies.

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Phosducin and βγ-Transducin Interaction I: Effects of Post-translational Modifications

Cited by 28 publications

References 27 publications

Modulation of CRX Transactivation Activity by Phosducin Isoforms

Modulation of CRX Transactivation Activity by Phosducin Isoforms

Phosducin interacts with the G-protein βγ-dimer of ciliate protozoanBlepharisma japonicumupon illumination

The physiological roles of phosducin: from retinal function to stress-dependent hypertension

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