当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > Cloning and characterization of mouse disabled 2 interacting protein 2, a mouse orthologue of human NOSTRIN.

Cloning and characterization of mouse disabled 2 interacting protein 2, a mouse orthologue of human NOSTRIN.

Abstract：

:The mouse disabled 2 interacting protein 2 (mDaIP2) had been obtained through yeast two hybrid system. It consists of 506 amino acids and its calculated molecular weight is 57.7 kDa. The protein contains N-terminal FCH domain and C-terminal SH3 domain. The SH3 domain interacts with the proline rich domain of mDab2 which had been identified to possess a transcriptional activation function. In RA-treated F9 teratocarcinoma cell, the mDaIP2 and mDab2 genes were differentially expressed in a RA-responsive manner and both were detected to localize in cytoplasm and nucleus. Homology search of all NCBI sequences indicated that the amino acid sequence of mDaIP2 shares 82% identity with human NOSTRIN which controls activity, trafficking, and targeting of nitric oxide synthase (eNos). The eNos was not detected in RA-treated F9 cell. These results suggest that mDaIP2 somehow functions in a different fashion from NOSTRIN in F9 cell differentiation and that its function may be concerted with that of mDab2.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Choi YJ,Cho SY,Kim HW,Kim JA,Bae SH,Park SS

doi

10.1016/j.bbrc.2004.11.079

subject

Has Abstract

pub_date

2005-01-21 00:00:00

pages

594-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)02622-1

journal_volume

326

pub_type

杂志文章

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