Article
Scmh1 has E3 ubiquitin ligase activity for geminin and histone H2A and regulates geminin stability directly or indirectly via transcriptional repression of Hoxa9 and Hoxb4.
Molecular and cellular biology - 1 Feb 2013
Yasunaga Shin'ichiro, Ohtsubo Motoaki, Ohno Yoshinori, Saeki Keita, Kurogi Toshiaki, Tanaka-Okamoto Miki, Ishizaki Hiroyoshi, Shirai Manabu, Mihara Keichiro, Brock Hugh W, Miyoshi Jun, Takihara Yoshihiro
Abstract excerpt
Polycomb-group (PcG) complex 1 acts as an E3 ubiquitin ligase both for histone H2A to silence transcription and for geminin to regulate its stability. Scmh1 is a substoichiometric component of PcG complex 1 that provides the complex with an interaction domain for geminin. Scmh1 is unstable and regulated through the ubiquitin-proteasome system, but its molecular roles are unknown, so we generated Scmh1-deficient...
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