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Gene Review:

KAPP - kinase associated protein phosphatase

Arabidopsis thaliana

Synonyms: RAG1, ROOT ATTENUATED GROWTH 1, T24G5.3

Shah, K. et al., Williams, R.W. et al., Stone, J.M. et al., Gómez-Gómez, L. et al., Rienties, I.M. et al.

Gómez-Gómez, Bauer, Boller,

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High impact information on KAPP

The phosphatase, designated KAPP (kinase-associated protein phosphatase), is composed of three domains: an amino-terminal signal anchor, a kinase interaction (KI) domain, and a type 2C protein phosphatase catalytic region [1].
These results suggest that KAPP is an integral part of the AtSERK1 endocytosis mechanism [2].
AtSERK1(T463A)-CFP and AtSERK1(3T-->A)-CFP proteins were partially sequestered intracellularly in the absence of KAPP-YFP protein, suggesting an active role for KAPP dephosphorylation of threonine residues in the AtSERK1 A-loop in receptor internalization [2].
Using mutant AtSERK1 proteins in which Thr 462, Thr 463, and Thr 468 in the A-loop of the AtSERK1 kinase domain were replaced by alanines, we show that phosphorylation status of the receptor is involved in interaction with KAPP [2].
The Arabidopsis kinase-associated protein phosphatase controls internalization of the somatic embryogenesis receptor kinase 1 [2].

Biological context of KAPP

We present a model where KAPP functions as a negative regulator of the CLAVATA1 signal transduction pathway [3].
Overexpression of KAPP mimics the clv1 mutant phenotype [3].

Anatomical context of KAPP

Both KAPP and AtSERK1 proteins are found at the plasma membrane [2].

Physical interactions of KAPP

Our results show that AtSERK1 interacts with the kinase-associated protein phosphatase (KAPP) in vitro [2].

Enzymatic interactions of KAPP

Finally, KAPP binds and dephosphorylates CLV1 [3].

Other interactions of KAPP

Furthermore, using the yeast two-hybrid system, we show physical interaction of KAPP with the kinase domain of FLS2 [4].
Furthermore, CLV1 has kinase activity: it phosphorylates both itself and KAPP [3].
In yeast, AtCDC48 interacts with GF14lambda and with the PP2C phosphatase KAPP [5].

References

Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase. Stone, J.M., Collinge, M.A., Smith, R.D., Horn, M.A., Walker, J.C. Science (1994) [Pubmed]
The Arabidopsis kinase-associated protein phosphatase controls internalization of the somatic embryogenesis receptor kinase 1. Shah, K., Russinova, E., Gadella, T.W., Willemse, J., De Vries, S.C. Genes Dev. (2002) [Pubmed]
A possible role for kinase-associated protein phosphatase in the Arabidopsis CLAVATA1 signaling pathway. Williams, R.W., Wilson, J.M., Meyerowitz, E.M. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis. Gómez-Gómez, L., Bauer, Z., Boller, T. Plant Cell (2001) [Pubmed]
The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP. Rienties, I.M., Vink, J., Borst, J.W., Russinova, E., de Vries, S.C. Planta (2005) [Pubmed]

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