2006
DOI: 10.1074/jbc.m513703200
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SUMO-1 Controls the Protein Stability and the Biological Function of Phosducin

Abstract: Phosducin regulates Gbetagamma-stimulated signaling by binding to Gbetagamma subunits of heterotrimeric G-proteins. Control of phosducin activity by phosphorylation is well established. However, little is known about other mechanisms that may control phosducin activity. Here we report that phosducin is regulated at the posttranslational level by modification with the small ubiquitin-related modifier, SUMO. We demonstrate modification with SUMO for phosducin in vitro expressed in cells and for native phosducin … Show more

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Cited by 61 publications
(43 citation statements)
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“…As previously reported, sumoylation-competent phd remained stable over time while the sumoylation-deficient phd K33R protein underwent degradation (Fig. 4A, top) (24). In contrast, both NP and NP K4,7R protein levels remained stable under CHX treatment (Fig.…”
Section: Resultssupporting
confidence: 61%
“…As previously reported, sumoylation-competent phd remained stable over time while the sumoylation-deficient phd K33R protein underwent degradation (Fig. 4A, top) (24). In contrast, both NP and NP K4,7R protein levels remained stable under CHX treatment (Fig.…”
Section: Resultssupporting
confidence: 61%
“…SUMOylation stabilizes dengue virus NS5 against proteasome degradation, which supports virus replication (72). SUMO-1 stabilizes phosducin, and the authors inferred that SUMO moieties conjugated on phosducin may mask the region recognized by the ubiquitin-proteasome pathway (75). Following gradient overexpression of SUMO-1 and Ubc9 or SENP-1 with 3D, the results showed that the level of ubiquitination was highly dependent on SUMOylation.…”
Section: Discussionmentioning
confidence: 72%
“…Pdc expression approaches GÎČÎł expression only in the retina and pineal gland, while in other tissues its expression levels are vanishingly low [50]. Thus, there appears to be insufficient Pdc in most cells to sequester enough GÎČÎł to impact G protein signaling significantly.…”
Section: Modifying the Model -New Clues About Pdc Functionmentioning
confidence: 98%
“…A small fraction of the total Pdc appears to be localized in the nucleus [45,59], a Pdc C-terminal fragment has been reported to act as a transcription activator [60] and Pdc binds to the photoreceptor-specific transcription factor CRX in vitro [61]. In addition, Pdc has recently been shown to be SUMOylated and SUMOylation machinery has been shown to associate with the nuclear pore complex that imports proteins into the nucleus [50]. Finally, localization studies indicate that Pdc is more concentrated in the synaptic terminus of rods, perhaps suggesting a role for Pdc in synaptic transmission [45].…”
Section: Current Thinking -Pdc As a Chaperone Of Light-dependent G T mentioning
confidence: 99%