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Dev Cell 2003 Mar 01;43:419-29. doi: 10.1016/s1534-5807(03)00036-4.
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The cytoplasmic domain of Xenopus NF-protocadherin interacts with TAF1/set.

Heggem MA , Bradley RS .

Protocadherins are members of the cadherin superfamily of cell adhesion molecules proposed to play important roles in early development, but whose mechanisms of action are largely unknown. We examined the function of NF-protocadherin (NFPC), a novel cell adhesion molecule essential for the histogenesis of the embryonic ectoderm in Xenopus, and demonstrate that the cellular protein TAF1, previously identified as a histone-associated protein, binds the NFPC cytoplasmic domain. NFPC and TAF1 coprecipitate from embryo extracts when ectopically expressed, and TAF1 can rescue the ectodermal disruptions caused by a dominant-negative NFPC construct lacking the extracellular domain. Furthermore, disruptions in either NFPC or TAF1 expression, using NFPC- or TAF1-specific antisense morpholinos, result in essentially identical ectodermal defects. These results indicate a role for TAF1 in the differentiation of the embryonic ectoderm, as a cytosolic cofactor of NFPC.

PubMed ID: 12636922
Article link: Dev Cell
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: pcdh7 set taf1
Antibodies: Pcdh7 Ab1 Set Ab2 Set Ab3
Morpholinos: pcdh7 MO1 set MO1

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