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Special Issue "Protein SUMOylation"
A special issue of Biomolecules (ISSN 2218-273X).
Deadline for manuscript submissions: closed (28 February 2012).
Fax: (410) 502-1872
Interests: transcriptional control of neural and glial development; protein SUMOylation; noncoding RNAs; functional proteomics; chronobiology
SUMOylation has emerged as a reversible and widely used means of modulating the activity and localization of many different classes of protein. Originally thought to primarily regulate nuclear processes such as transcription and DNA repair, recent work has revealed that SUMOylation plays a critical role in such diverse functions as regulating kinase and G-protein activity, cytoskeletal structure and ion channel function. It is now appreciated that site-specific SUMOylation guides cellular differentiation, regulates neuronal activity, and is misregulated in a range of human diseases. This issue intends to both review recent findings and to showcase original research in this fast moving field.
We thus invite submission of research and review manuscripts that cover any aspect of the biochemistry, cell biology, genetics or pharmacology of SUMO, SUMOylation enzymes and their cellular substrates and effector molecules. Areas of particular interest include, but are not limited to, advances in SUMOylation-dependent regulation of transcription factor activity and chromatin structure, dynamic regulation of SUMOylation by intracellular signaling, novel functional classes of proteins regulated by SUMOylation, and the role of SUMOylation in embryonic development, cancer and neurodegeneration. Other potential topics include the biology of the growing number of E3 SUMO ligases, SUMO binding proteins, and new genetic and pharmacological techniques for modulating protein SUMOylation in vivo.
We look forward to reading your contributions,
Prof. Dr. Seth Blackshaw
- SUMO and SUMOylation
- development and differentiation
- ion channel and synapse
- proteomics cell dynamics
- Transcription and gene expression
- protein transport stability and structure
- ubiquitin, acetylation, phosphorylation, and post-translational modification
- chromatin and epigenetics
- signal transduction