Pechlivanis, Markos and Samol, Annette and Kerkhoff, Eugen (2009) Identification of a Short Spir Interaction Sequence at the C-terminal End of Formin Subgroup Proteins. JOURNAL OF BIOLOGICAL CHEMISTRY, 284 (37). pp. 25324-25333. ISSN 0021-9258, 1083-351X
Full text not available from this repository. (Request a copy)Abstract
The actin nucleation factors Spire and Cappuccino interact with each other and regulate essential cellular events during Drosophila oogenesis in a cooperative fashion. The interaction blocks formin actin nucleation activity and enhances the Spire activity. Analogous to Spire and Cappuccino, the mammalian homologs Spir-1 and formin-2 show a regulatory interaction. To get an understanding of the nature of the Spir-formin cooperation, we have analyzed the interaction biochemically and biophysically. Our data shows that the association of Spir-1 and formin-2 is not significantly mediated by binding of the Spir-1-KIND domain to the formin FH2 core domain. Instead, a short sequence motif C-terminal adjacent to the formin-2-FH2 domain could be characterized that mediates the interaction and is conserved among the members of the Fmn subgroup of formins. In line with this, we found that both mammalian Spir proteins, Spir-1 and Spir-2, interact with mammalian Fmn subgroup proteins formin-1 and formin-2.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | LOCALIZED MESSENGER-RNA; ACTIN NUCLEATION FACTOR; MOUSE OOCYTES; CAPPUCCINO; SPINDLE; EMBRYO; DOMAINS; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 07 Sep 2020 08:11 |
| Last Modified: | 07 Sep 2020 08:11 |
| URI: | https://pred.uni-regensburg.de/id/eprint/28410 |
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