| First Author | Sorenson CM | Year | 2004 |
| Journal | J Biol Chem | Volume | 279 |
| Issue | 12 | Pages | 11368-74 |
| PubMed ID | 14699151 | Mgi Jnum | J:88736 |
| Mgi Id | MGI:3036971 | Doi | 10.1074/jbc.M310079200 |
| Citation | Sorenson CM (2004) Interaction of bcl-2 with Paxillin through its BH4 domain is important during ureteric bud branching. J Biol Chem 279(12):11368-74 |
| abstractText | bcl-2 protects cells from apoptosis initiated by a variety of stimuli including loss of cell adhesion. Mice deficient in bcl-2 (bcl-2-/-) develop renal hypoplastic/cystic dysplasia, a condition that leads to significant morbidity and mortality in children. The precise mechanism of action of bcl-2 has not been elucidated. bcl-2 may merely facilitate survival of precursor cells and/or may play a more 'active' role during morphogenesis by interacting with other proteins such as paxillin. Recent work in this laboratory demonstrated that bcl-2 directly associates with paxillin. The data presented here demonstrate that the bcl-2 homology 4 (BH4) domain, specifically amino acids 17-31, is necessary for the bcl-2 interaction with paxillin. Paxillin also associated with the BH4 domains of more closely related bcl-2 family members, bcl-xL and bcl-w, compared with that from the non-mammalian homologue ced9. Tyrosines 21 and 28 in the bcl-2 BH4 domain were essential for interaction with paxillin. In embryonic kidney organ culture, incubation with the bcl-2 BH4 domain resulted in inhibition of ureteric bud branching. Therefore, these data suggest that the interaction of bcl-2 with paxillin plays an important role during nephrogenesis. |
