Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties

原肌球蛋白 II 可进行选择性剪接,从而产生差异表达且具有不同生化特性的原肌球蛋白异构体

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作者:A Lambrechts, A Braun, V Jonckheere, A Aszodi, L M Lanier, J Robbens, I Van Colen, J Vandekerckhove, R Fässler, C Ampe

Abstract

We deduced the structure of the mouse profilin II gene. It contains five exons that can generate four different transcripts by alternative splicing. Two transcripts encode different profilin II isoforms (designated IIa and IIb) that have similar affinities for actin but different affinities for polyphosphoinositides and proline-rich sequences. Profilins IIa and IIb are also present in humans, suggesting that all mammals have three profilin isoforms. Profilin I is the major form in all tissues, except in the brain, where profilin IIa is most abundant. Profilin IIb appears to be a minor form, and its expression is restricted to a limited number of tissues, indicating that the alternative splicing is tightly regulated. Western blotting and whole-mount in situ hybridization show that, in contrast to the expression of profilin I, the expression level of profilin IIa is developmentally regulated. In situ hybridization of adult brain sections reveals overlapping expression patterns of profilins I and IIa.

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