Distinct functions of human MVB12A and MVB12B in the ESCRT-I dependent on their posttranslational modifications

Biochemical and Biophysical Research Communications
Takumi TsunematsuHiroaki Konishi

Abstract

ESCRT-I, which mediates the sorting of ubiquitinated cargo protein from the plasma membrane to the endosomal vesicle, comprises a heterotetramer of TSG101 (Vps23), Vps28, Vps37 and MVB12 protein. In humans, the structurally similar subtypes MVB12A and MVB12B are subunits of ESCRT-I. However, no functional description of these proteins has been described. Here we show the differing effects of tyrosine phosphorylation and ubiquitination of both MVB12 proteins on their respective functions. As noted in our previous study, Tyr204 phosphorylation of MVB12A in response to epidermal growth factor (EGF) stimulation affects binding to CD2AP, which regulates the amounts of EGF receptor bound to ESCRT-I. Strikingly, ubiquitination of Lys264 and Lys290 of MVB12B was induced and led to the instability and inclusion of MVB12B in COS-7 cells. These ubiquitinations increased upon EGF stimulation, which was regulated by the phosphorylations of Tyr241 and Tyr243 of MVB12B. Furthermore, MVB12A was also involved in the aggregation-prone proteins of MVB12B. These results suggest that the expression of MVB12B may be normally suppressed through the ubiquitin-proteasome pathway that simultaneously regulates the fate of MVB12A and the functions of ESCR...Continue Reading

References

May 26, 2005·Biochimica Et Biophysica Acta·Katherine Bowers, Tom H Stevens
Oct 18, 2005·Nature Reviews. Molecular Cell Biology·Mirko H H Schmidt, Ivan Dikic
Aug 10, 2006·The Journal of Biological Chemistry·Hiroaki KonishiHisaaki Taniguchi
Dec 6, 2006·The Journal of Cell Biology·Tony ChuScott D Emr
Apr 24, 2007·Nature Reviews. Molecular Cell Biology·Roger L Williams, Sylvie Urbé
Jun 9, 2007·Science·Jez G Carlton, Juan Martin-Serrano
Apr 22, 2009·The Journal of Cell Biology·S Brookhart ShieldsRobert Piper
Jun 19, 2009·Journal of Cell Science·Tor Erik Rusten, Harald Stenmark

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Citations

Dec 24, 2011·Nature Cell Biology·Tor Erik RustenHarald Stenmark
Mar 27, 2013·Annual Review of Biochemistry·John McCulloughWesley I Sundquist
Nov 29, 2013·Journal of Cell Science·Lydia WunderleyPhilip Woodman
Jan 19, 2011·The Journal of Cell Biology·Daniel K Stringer, Robert C Piper
Jul 28, 2013·Marine Biotechnology·Carlos Frederico Ceccon LanesIgor Babiak
Jul 16, 2011·Current Biology : CB·Flavia StefaniPhilip Woodman
Jul 19, 2011·Developmental Cell·William M HenneScott D Emr
Jan 26, 2020·Toxicology in Vitro : an International Journal Published in Association with BIBRA·Charles O'DohertyRichard Murphy
Mar 13, 2012·Structure·Natasha Pashkova, Robert C Piper

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