Sumoylation of internally initiated Sp3 isoforms regulates transcriptional repression via a Trichostatin A-insensitive mechanism.

Spengler, Mary L

Sumoylation of internally initiated Sp3 isoforms regulates transcriptional repression via a Trichostatin A-insensitive mechanism. [electronic resource] - Cellular signalling Feb 2005 - 153-66 p. digital

Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.

0898-6568

10.1016/j.cellsig.2004.06.007 doi


Amino Acid Substitution
Animals
Blotting, Western
COS Cells
Cell Line
Cell Line, Tumor
Cell Nucleus--chemistry
Chlorocebus aethiops
DNA-Binding Proteins--chemistry
Enzyme Inhibitors--pharmacology
Ethylmaleimide--chemistry
Humans
Hydroxamic Acids--pharmacology
Immunohistochemistry
Lysine--metabolism
Neoplasm Proteins--genetics
Nuclear Proteins--genetics
Promoter Regions, Genetic--genetics
Promyelocytic Leukemia Protein
Prostate-Specific Antigen--genetics
Protein Isoforms--genetics
SUMO-1 Protein--genetics
Sp1 Transcription Factor--chemistry
Sp3 Transcription Factor
Tetrahydrofolate Dehydrogenase--genetics
Transcription Factors--chemistry
Transcriptional Activation--drug effects
Transfection
Tumor Suppressor Proteins
Two-Hybrid System Techniques
Ubiquitin-Conjugating Enzymes--metabolism
Ubiquitin-Conjugating Enzyme UBC9