title: The cytoplasmic domain of Xenopus NF-protocadherin interacts with TAF1/set.
abstract: 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.
authors.affiliation: Department of Cell Biology and Neuroscience, Montana State University, Bozeman, MT 59717, USA.
authors.forename: Mike A
authors.initials: MA
authors.lastname: Heggem
authors.forename: Roger S
authors.initials: RS
authors.lastname: Bradley
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D016375:Antisense Elements (Genetics); D017209:Apoptosis / Q000187:drug effects / Q000235:genetics; D015820:Cadherins / Q000235:genetics / Q000378:metabolism*; D002454:Cell Differentiation / Q000235:genetics; D002868:Chromosomal Proteins, Non-Histone / Q000235:genetics / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism*; D004268:DNA-Binding Proteins; D004475:Ectoderm / Q000166:cytology / Q000378:metabolism*; D004625:Embryo, Nonmammalian / Q000196:embryology* / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental / Q000235:genetics; D006367:HeLa Cells; D056488:Histone Chaperones; D006801:Humans; D007150:Immunohistochemistry; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics; D000091363:Protocadherins; D012333:RNA, Messenger / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000235:genetics; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D029867:Xenopus Proteins; D014982:Xenopus laevis / Q000196:embryology* / Q000378:metabolism
chemical_list: D016375:Antisense Elements (Genetics); D015820:Cadherins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D056488:Histone Chaperones; C112030:PCDH7 protein, Xenopus; D000091363:Protocadherins; D012333:RNA, Messenger; D011993:Recombinant Fusion Proteins; C513473:SET protein, human; D014157:Transcription Factors; D029867:Xenopus Proteins