Cloning and Characterization of BAP3 (BAI-Associated Protein 3), a C2 Domain-Containing Protein That Interacts with BAI1

1998 ◽  
Vol 251 (1) ◽  
pp. 158-165 ◽  
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Katsutoshi Oda ◽  
Hiroyuki Nishimori ◽  
Mikio Suzuki ◽  
Eiichi Takahashi ◽  
...  
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Chunying Li ◽  
Zhe Liang ◽  
Hao Yu

Biochemistry ◽  
2003 ◽  
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Senena Corbalán-Garcia ◽  
Susana Sánchez-Carrillo ◽  
Josefa García-García ◽  
Juan C. Gómez-Fernández

2013 ◽  
Vol 35 (9) ◽  
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Yongsheng Cao ◽  
Di Li ◽  
Chong Cao ◽  
Mingchun Gao ◽  
Runxiang Zhang ◽  
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Planta ◽  
2008 ◽  
Vol 227 (5) ◽  
pp. 1169-1179 ◽  
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Soo-Yong Kim ◽  
Doil Choi ◽  
Choong-Min Ryu ◽  
Jeong Mee Park

2009 ◽  
Vol 23 (S1) ◽  
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Marta Guerrero‐Valero ◽  
Cristina Ferrer‐Orta ◽  
Jordi Querol‐Audi ◽  
Consuelo Marin‐Vicente ◽  
...  

2020 ◽  
Vol 148 ◽  
pp. 180-192
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Mohd Sabri Pak Dek ◽  
Priya Padmanabhan ◽  
Krishnaraj Tiwari ◽  
James F. Todd ◽  
Gopinadhan Paliyath

1998 ◽  
Vol 244 (2) ◽  
pp. 531-539 ◽  
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Motoaki Ohtsubo ◽  
Neal G. Copeland ◽  
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Nancy A. Jenkins ◽  
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1997 ◽  
Vol 326 (1) ◽  
pp. 139-147 ◽  
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Jan DOMIN ◽  
Françoise PAGES ◽  
Stefano VOLINIA ◽  
Susan E. RITTENHOUSE ◽  
Marketa J. ZVELEBIL ◽  
...  

The generation of phosphatidylinositide 3-phosphates has been observed in a variety of cellular responses. The enzymes that mediate synthesis are the phosphoinositide 3-kinases (PI3-Ks) that form a family of structurally diverse enzymes with distinct substrate specificities. In this paper, we describe the cloning of a novel human PI3-K, namely PI3-K-C2α, which contains a C-terminal C2 domain. This enzyme can be assigned to the class II PI3-Ks, which was defined by characterization of the Drosophila 68D enzyme and includes the recently described murine enzymes m-cpk and p170. Despite the overall similarity in the amino acid sequence of the murine and human enzymes, which suggests that they are encoded by closely related genes, these molecules show marked sequence heterogeneity at their N-termini. Biochemical analysis of recombinant PI3-K-C2α demonstrates a restricted lipid substrate specificity. As reported for other members of this class, the enzyme only phosphorylates PtdIns and PtdIns4P when the lipids are presented alone. However, when lipids were presented together with phosphatidylserine acting as a carrier, phosphorylation of PtdIns(4,5)P2 was also observed. The catalytic activity of PI3-K-C2α is refractory to concentrations of wortmannin and LY294002 which inhibit the PI3-K activity of other family members. The comparative insensitivity of PI3-K-C2α to these inhibitors suggests that their use should be re-evaluated in the study of PI3-Ks.


2013 ◽  
Vol 57 (4) ◽  
pp. 701-710 ◽  
Author(s):  
G. Zhang ◽  
Y. F. Sun ◽  
Y. M. Li ◽  
Y. L. Dong ◽  
X. L. Huang ◽  
...  

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