期刊论文详细信息
FEBS Letters
Identification and molecular characterization of BP75, a novel bromodomain‐containing protein
Hendriks, Wiljan1  Pepers, Barry1  van Ham, Marco1  Cuppen, Edwin1  Wieringa, Bé1 
[1] Department of Cell Biology, Institute of Cellular Signalling, University of Nijmegen, Adelbertusplein 1, 6525 EK Nijmegen, The Netherlands
关键词: Protein-protein interaction;    Protein tyrosine phosphatase;    Bromodomain;    Signalling;    BP75;    bromodomain protein of 75 kDa;    BYC;    acronym for BP75;    YN92 and C01H6.7;    PTP-BL;    protein tyrosine phosphatase-BAS-like;    PDZ;    acronym for post-synaptic density protein PSD-95;    Drosophila discs large tumor suppressor DlgA and the tight junction protein ZO-1;   
DOI  :  10.1016/S0014-5793(99)01191-6
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

We here describe the identification and characterization of a novel bromodomain-containing protein, the bromodomain protein of 75 kDa (BP75). Initially, we identified BP75 in a two-hybrid screening for proteins that interact with the first PDZ (acronym for post-synaptic density protein PSD-95, Drosophila discs large tumor suppressor DlgA and the tight junction protein ZO-1) domain in protein tyrosine phosphatase-BAS-like (PTP-BL). We found that BP75 is expressed ubiquitously and show that both BP75 and a PTP-BL deletion mutant consisting of the first PDZ domain are located mainly in the nucleus, although cytoplasmic localization is also evident. Full-length PTP-BL, on the contrary, is predominantly localized in the cytoplasm, although some basal nuclear staining is observed. The described molecular interaction may reflect a mechanism of coupling submembraneous signalling events and nuclear events.

【 授权许可】

Unknown   

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