Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
J Bies, J Markus, L Wolff - Journal of Biological Chemistry, 2002 - ASBMB
The transcription factor c-Myb is subject to several types of post-translational modifications,
including phosphorylation, acetylation, and ubiquitination. These modifications regulate the
transcription and transforming activity as well as the proteolytic stability of c-Myb. Here we
report the covalent modification of c-Myb with the small ubiquitin-related protein SUMO-1.
Mutational analysis identified two major sumolation sites (Lys 499 and Lys 523) in the
negative regulatory domain. Interestingly, the single mutation K523R completely abolished …
including phosphorylation, acetylation, and ubiquitination. These modifications regulate the
transcription and transforming activity as well as the proteolytic stability of c-Myb. Here we
report the covalent modification of c-Myb with the small ubiquitin-related protein SUMO-1.
Mutational analysis identified two major sumolation sites (Lys 499 and Lys 523) in the
negative regulatory domain. Interestingly, the single mutation K523R completely abolished …
