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Review
. 2016 Jul;62(5):496-509.
doi: 10.18097/PBMC20166205496.

[Atypical ubiquitination of proteins]

[Article in Russian]
O A Buneeva  1 , A E Medvedev  1
Affiliations
Review

[Atypical ubiquitination of proteins]

[Article in Russian]
O A Buneeva et al. Biomed Khim. 2016 Jul.

Abstract
in English, Russian

Ubiquitination is a type of posttranslational modification of intracellular proteins characterized by covalent attachment of one (monoubiquitination) or several (polyubiquitination) of ubiquitin molecules to target proteins. In the case of polyubiquitination, linear or branched polyubiquitin chains are formed. Their formation involves various lysine residues of monomeric ubiquitin. The best studied is Lys48-polyubiquitination, which targets proteins for proteasomal degradation. In this review we have considered examples of so-called atypical polyubiquitination, which mainly involves other lysine residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys63) and also N-terminal methionine. The considered examples convincingly demonstrate that polyubiquitination of proteins not necessarily targets proteins for their proteolytic degradation in proteasomes. Atypically polyubiquitinated proteins are involved in regulation of various processes and altered polyubiquitination of certain proteins is crucial for development of serious diseases.

Ubikvitinirovanie – raznovidnost' posttransliatsionnoĭ modifikatsii vnutrikletochnykh belkov, v khode kotoroĭ proiskhodit kovalentnoe prisoedinenie molekul ubikvitina k belkam-misheniam. Razlichaiut monoubikvitinirovanie (prisoedinenie odnoĭ molekuly ubikvitina), mnozhestvennoe monoubikvitinirovanie (tak nazyvaemoe mul'tiubikvitinirovanie) i poliubikvitinirovanie (prisoedinenie k belku-misheni tsepochki, sostoiashcheĭ iz neskol'kikh (chashche vsego chetyrekh) molekul ubikvitina. V sluchae poliubikvitinirovaniia obrazuiutsia lineĭnye ili razvetvlennye tsepi polimernykh form étogo belka. V ikh obrazovanii uchastvuiut razlichnye ostatki lizina monomerov ubikvitina. Naibolee khorosho izucheno poliubikvitinirovanie s uchastiem Lys48, kotoroe chashche vsego privodit k dostavke belkov-misheneĭ dlia proteoliticheskoĭ degradatsii. V dannom obzore rassmotreny primery t.n. atipichnogo poliubikvitinirovaniia s uchastiem drugikh ostatkov lizina (Lys6, Lys11, Lys27, Lys29, Lys33, Lys63) i N-kontsevogo ostatka metionina. Éti primery ubeditel'no svidetel'stvuiut o tom, chto poliubikvitinirovanie belkov-misheneĭ daleko ne vsegda privodit k ikh proteoliticheskoĭ degradatsii. Poliubikvitinirovannye belki uchastvuiut v reguliatsii samykh raznykh kletochnykh protsessov, vkliuchaia immunnyĭ otvet, stabil'nost' genoma, peredachu signala i drugie. Narusheniia mekhanizmov ubikvitinirovaniia vedut k vozniknoveniiu razlichnykh zabolevaniĭ.

Keywords: atypical ubiquitination; posttranslational modification of proteins; ubiquitin; ubiquitination enzymes.

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