| First Author | Keicher C | Year | 2004 |
| Journal | Biochem Biophys Res Commun | Volume | 324 |
| Issue | 1 | Pages | 308-16 |
| PubMed ID | 15465019 | Mgi Jnum | J:93130 |
| Mgi Id | MGI:3056009 | Doi | 10.1016/j.bbrc.2004.08.235 |
| Citation | Keicher C, et al. (2004) Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase. Biochem Biophys Res Commun 324(1):308-16 |
| abstractText | LIM and SH3 domain protein (LASP-1) is a specific focal adhesion protein involved in cell migration. Overlay studies demonstrate that LASP-1 directly binds to the proline-rich domains of zyxin, lipoma preferred partner (LPP), and vasodilator-stimulated phosphoprotein (VASP), with zyxin being the most prominent interacting partner. Despite the LIM/zinc-finger domain, hypothesized to be involved in homodimerization, LASP-1 exists as a monomer. In vitro phosphorylation of recombinant mouse LASP-1 by cAMP- and cGMP-dependent protein kinase (PKA and PKG, respectively) occurs at serine 61, serine 99, and threonine 156 whereas in intact cells mouse LASP-1 is phosphorylated only at threonine 156. This site is different from the known in vivo phosphorylation sites in human (serine 146) and rabbit (serine 99 and serine 146). Nevertheless, immunofluorescence of LASP-1 in human and mouse mesangial cells revealed no difference in subcellular distribution. Exposure of the cells to forskolin induced a translocation of both, human and mouse LASP-1, from the focal contacts to the cell interior without affecting F-actin structure. Immunoblotting of LASP-1 in various mouse and human tissues detected a similar prominent expression in non-muscle tissue. Altogether, our data suggest so far no functional differences between human and mouse LASP-1. |
