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Vol. 16, No. 13, pp. 1707-1720, July 1, 2002
Laboratory of Molecular Biology, Department of Plant Sciences,
Wageningen University, 6703 HA Wageningen, The Netherlands
The AtSERK1 protein is a plasma membrane-located LRR
receptor-like serine threonine kinase that is transiently expressed
during plant embryogenesis. Our results show that AtSERK1
interacts with the kinase-associated protein phosphatase (KAPP) in
vitro. The kinase interaction (KI) domain of KAPP does not interact
with a catalytically inactive kinase mutant. 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. KAPP and AtSERK1 cDNAs were fused to two
different variants of green fluorescent protein (GFP), the yellow
fluorescent protein (YFP) or the cyan fluorescent protein (CFP). Both
KAPP and AtSERK1 proteins are found at the plasma membrane. Our
results show that AtSERK1-CFP becomes sequestered into
intracellular vesicles when transiently coexpressed with KAPP-YFP
proteins. AtSERK1T463A-CFP and
AtSERK13T
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. The interaction
between the KAPP-CFP/YFP and AtSERK1-CFP/YFP fusion proteins
was investigated with fluorescence spectral imaging microscopy (FSPIM).
Our results show that AtSERK1-CFP and KAPP-YFP proteins are
colocalized at the plasma membrane but only show fluorescence energy
transfer (FRET) indicative of physical interaction in intracellular
vesicles. These results suggest that KAPP is an integral part of the
AtSERK1 endocytosis mechanism.
[Key Words: Interaction; phosphorylation; localization; fluorescence; phosphatase]
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