Kathleen A. Gallo Research Interests continued
MLK3 contains several potential protein-protein interactions domains
that likely contribute to its regulation and signaling specificity, including
an N-terminal SH3 domain, a centrally located zipper and a Cdc42/Rac Interactive
Binding (CRIB) motif, and a C-terminal region with a preponderance of serine,
threonine, and proline residues. Work in our lab indicates that MLK3 is
autoinhibited through an interaction between its SH3 domain and a noncanonical
SH3 binding motif that is situated between the zipper and CRIB motifs. We
have also found that activated forms of the small GTPases Cdc42 and Rac
increase MLK3's autophosphorylation and substrate phosphorylation activity,
change the subcellular localization of MLK3, and are correlated with changes
in MLK3's in vivo phosphorylation status.
The Gallo Laboratory uses biochemical, biophysical and cell biological approaches-including
confocal microscopy and mass spectrometry- towards understanding the molecular
mechanisms that regulate MLKs and their signaling pathways.
Full text of research interests