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Control of Meristem Development by CLAVATA1 Receptor Kinase and Kinase-Associated Protein Phosphatase Interactions1

Julie M. Stone2, 3, Amy E. Trotochaud2, John C. Walker, and Steven E. Clark*

Division of Biological Sciences, University of Missouri, Columbia, Missouri 65211-7400 (J.M.S., J.C.W.); and Department of Biology, University of Michigan, Ann Arbor, Michigan 48109-1048 (A.E.T., S.E.C.)

The CLAVATA1 (CLV1) gene encodes a putative receptor kinase required for the proper balance between cell proliferation and differentiation in Arabidopsis shoot and flower meristems. Impaired CLV1 signaling results in masses of undifferentiated cells at the shoot and floral meristems. Although many putative receptor kinases have been identified in plants, the mechanism of signal transduction mediated by plant receptor-like kinases is largely unknown. One potential effector of receptor kinase signaling is kinase-associated protein phosphatase (KAPP), a protein that binds to multiple plant receptor-like kinases in a phosphorylation-dependent manner. To examine a possible role for KAPP in CLV1-dependent plant development, the interaction of CLV1 and KAPP was investigated in vitro and in vivo. KAPP binds directly to autophosphorylated CLV1 in vitro and co-immunoprecipitates with CLV1 in plant extracts derived from meristematic tissue. Reduction of KAPP transcript accumulation in an intermediate clv1 mutant suppresses the mutant phenotype, and the degree of suppression is inversely correlated with KAPP mRNA levels. These data suggest that KAPP functions as a negative regulator of CLV1 signaling in plant development. This may represent a general model for the interaction of KAPP with receptor kinases.

1   This work was supported by the National Science Foundation (NSF) (grant no. MCB-9417732 to J.C.W.), by the University of Missouri Food for the 21st Century Program (grant to J.C.W.), by the Department of Energy (DOE) (grant no. DE-FG02-96ER20227 to S.E.C.), and by the Triagency DOE/NSF/U.S. Department of Agriculture (Plant Biology Grant to Promote Collaboration in Plant Protein Phosphorylation no. 92-37105-7675).
2   J.M.S. and A.E.T. made equal contributions to this publication.
3   Present address: Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114.
*   Corresponding author; e-mail clarks{at}umich.edu; fax 1-734-647-0884.

Plant Physiol. (1998) 117: 1217-1225
Copyright Clearance Center:   0032-0889/98/117//09
© 1998 American Society of Plant Physiologists




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