Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism.
AffiliationCRC Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, UK. firstname.lastname@example.org
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AbstractThe Id family of helix-loop-helix proteins function as negative regulators of DNA binding, basic helix-loop-helix proteins in the regulation of cell growth and differentiation. We report here on the identification of a 17 kDa variant of the 14 kDa Id-3 protein termed Id-3L (long version) which possesses a unique 60 amino acid carboxy-terminus generated by read through of a 'coding intron' and alternative splicing. Northern analysis revealed expression of a minor 1.1 kb Id-3L transcript together with the predominant 0.95 kb Id-3 transcript in the majority of adult human tissues analysed. The variant Id-3L protein is functionally distinguishable from conventional Id-3 since in in vitro DNA mobility shift assays, it was greatly impaired in its ability to abrogate binding of the basic helix-loop-helix protein, E47, to an E box recognition sequence.
CitationAttenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism. 1996, 393 (1):113-6 FEBS Lett.
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