Binding of Drosophila Polo kinase to its regulator Matrimony is noncanonical and involves two separate functional domains.

Abstract:

:Drosophila melanogaster Polo kinase physically interacts with, and is repressed by, the Matrimony (Mtrm) protein during oogenesis. Females heterozygous for a deletion of the mtrm gene display defects in chromosome segregation at meiosis I. However, a complete absence of Mtrm results in both meiotic catastrophe and female sterility. We show that three phosphorylated residues in an N-terminal region in Mtrm are required for Mtrm::Polo binding. However, this binding is noncanonical; it does not require either a complete S-pS/pT-P motif in Mtrm or key residues in the Polo-box domain of Polo that allow Polo to bind phosphorylated substrates. By using fluorescence cross-correlation spectroscopy to characterize the Mtrm::Polo interaction in vivo, we show that a sterile α-motif (SAM) domain located at the C terminus of Mtrm increases the stability of Mtrm::Polo binding. Although Mtrm's C-terminal SAM domain is not required to rescue the chromosome segregation defects observed in mtrm/+ females, it is essential to prevent both meiotic catastrophe and the female sterility observed in mtrm/mtrm females. We propose that Polo's interaction with the cluster of phosphorylated residues alone is sufficient to rescue the meiosis I defect. However, the strengthening of Mtrm::Polo binding mediated by the SAM domain is necessary to prevent meiotic catastrophe and ensure female fertility. Characterization of the Mtrm::Polo interaction, as well as that of other Polo regulators, may assist in the design of a new class of Polo inhibitors to be used as targeted anticancer therapeutic agents.

authors

Bonner AM,Hughes SE,Chisholm JA,Smith SK,Slaughter BD,Unruh JR,Collins KA,Friederichs JM,Florens L,Swanson SK,Pelot MC,Miller DE,Washburn MP,Jaspersen SL,Hawley RS

doi

10.1073/pnas.1301690110

subject

Has Abstract

pub_date

2013-03-26 00:00:00

pages

E1222-31

issue

13

eissn

0027-8424

issn

1091-6490

pii

1301690110

journal_volume

110

pub_type

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