Post-translational modification by SUMO.

نویسندگان

  • Zara Hannoun
  • Sebastian Greenhough
  • Ellis Jaffray
  • Ronald T Hay
  • David C Hay
چکیده

Post-translational modifications (PTMs) are chemical alterations to a protein following translation, regulating stability and function. Reversible phosphorylation is an example of an important and well studied PTM involved in a number of cellular processes. SUMOylation is another PTM known to modify a large number of proteins and plays a role in various cellular processes including: cell cycle regulation, gene transcription, differentiation and cellular localisation. Therefore, understanding the role of SUMOylation in cell biology may allow the development of more efficient models, important in streamlining the drug discovery process. This review will focus on protein SUMOylation and its role in stem cell and somatic cell biology.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

SUMOylation and cell signalling.

SUMOylation is a highly transient post-translational protein modification. Attachment of SUMO to target proteins occurs via a number of specific activating and ligating enzymes that form the SUMO-substrate complex, and other SUMO-specific proteases that cleave the covalent bond, thus leaving both SUMO and target protein free for the next round of modification. SUMO modification has major effect...

متن کامل

Post-translational modification of POU domain transcription factor Oct-4 by SUMO-1.

POU domain transcription factor Oct-4 plays a crucial role in maintaining self-renewal and pluripotency of embryonic stem (ES) cells in a concentration-dependent manner. However, the molecular mechanism controlling Oct-4 levels in ES cells remains largely unknown. To explore the molecular mechanism regulating Oct-4 function, we constructed a mouse ES cell cDNA library and performed yeast two-hy...

متن کامل

SIZ1-Dependent Post-Translational Modification by SUMO Modulates Sugar Signaling and Metabolism in Arabidopsis thaliana.

Post-translational modification mechanisms function as switches that mediate the balance between optimum growth and the response to environmental stimuli, by regulating the activity of key proteins. SUMO (small ubiquitin-like modifier) attachment, or sumoylation, is a post-translational modification that is essential for the plant stress response, also modulating hormonal circuits to co-ordinat...

متن کامل

The post-translational modification, SUMOylation, and cancer (Review)

SUMOylation is a reversible post-translational modification which has emerged as a crucial molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune responses, carcinogenesis, cell cycle progression and apoptosis. Four SUMO isoforms have been identified, which are SUMO1, SUMO2/3 and SUMO4. The small ubiquitin-like modifier (SUMO) pathway is conserved in all eukaryo...

متن کامل

Regulation of Protein Function by SUMO Modification

SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is likely to be important. Control of the levels of SUMOylation is brought about through a balance of conjugating and deconjugating activities, i.e...

متن کامل

Predicting the protein SUMO modification sites based on Properties Sequential Forward Selection (PSFS).

Protein SUMO modification is an important post-translational modification and the optimization of prediction methods remains a challenge. Here, by using Support Vector Machines algorithm (SVM), a novel computational method was developed for SUMO modification site prediction based on Sequential Forward Selection (SFS) of hundreds of amino acid properties, which are collected by Amino Acid Index ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Toxicology

دوره 278 3  شماره 

صفحات  -

تاریخ انتشار 2010