β-微管蛋白属于微管蛋白亚家族,微管蛋白是微管的主要合成砌块。β-微管蛋白的分子量为55kDa。β−微管蛋白的结构特征在于具有被a--螺旋包围的两个β-折叠的核心。它还含有一个具有鸟嘌呤核苷酸结合区的N-末端结构域,一个具有紫杉醇结合位点的中间结构域,以及一个含有分子马达蛋白结合表面的C-末端结构域。人β-微管蛋白由七种亚型组成(β I (I类)、 β II (II类)、 β III (III类)、 β IVa (IVa类)、β IVb (IVb类)、β V (V类)和β VI (VI类)。
The unequal division of the CD blastomere at second cleavage is critical in establishing the second embryonic axis in the leech Helobdella, as in other unequally cleaving spiralians. When CD divides, the larger D and smaller C blastomeres arise invariantly
Structure of the alpha beta tubulin dimer by electron crystallography.
Molecular and cellular biology, 27(18), 6383-6395 (2007-07-20)
Studies of a TAZ knockout mouse reveal a novel function of the transcriptional regulator TAZ, that is, as a binding partner of the F-box protein beta-Trcp. TAZ-/- mice develop polycystic kidney disease (PKD) and emphysema. The calcium-permeable cation channel protein
Microtubules of the eukaryotic cytoskeleton are composed of a heterodimer of α- and β-tubulin. In addition to α-and β-tubulin, several other tubulins have been identified, bringing the number of distinct tubulin classes to seven.