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J Biol Chem, Vol. 273, Issue 5, 2698-2705, January 30, 1998
From the Protein Phosphorylation Laboratory, Imperial Cancer
Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, United
Kingdom and the § Ludwig Institute for Cancer Research,
University College London, Courtauld Building, 91 Riding House
Street, London W1P 8BT, United Kingdom
PRK1 (PKN) is a serine/threonine kinase that has
been shown to be activated by RhoA (Amano, M., Mukai, H., Ono, Y.,
Chihara, K., Matsui, T., Hamajima, Y., Okawa, K., Iwamatsu, A., and
Kaibuchi, K. (1996) Science 271, 648-650). Detailed
analysis of the PRK1 region involved in RhoA binding has revealed that
two homologous sequences within the HR1 domain (HR1a and HR1b) both
bind to RhoA; the third repeat within this domain,
HR1cPRK1, does not bind RhoA. The related HR1 motif is also
found to confer RhoA binding activity to the only other fully cloned
member of this kinase family, PRK2. Furthermore, the predictive value
of this motif is established for an HR1a sequence derived from a Caenorhabditis elegans open reading frame encoding a
protein kinase of unknown function. Interestingly, the
HR1aPRK1 and HR1bPRK1 subdomains are shown to
display a distinctive nucleotide dependence for RhoA binding.
HRIaPRK1 is entirely GTP-dependent, while
HR1bPRK1 binds both GTP- and GDP-bound forms of RhoA. This
distinction indicates that there are two sites of contact between RhoA
and PRK1, one contact through a region that is conformationally
dependent upon the nucleotide-bound state of RhoA and one that is not.
Analysis of binding to Rho/Rac chimera provides evidence for a
HR1aPRK1 but not HR1bPRK1 interaction in the
central third of Rho. Additionally, it is observed that the V14RhoA
mutant binds HR1a but does not bind HR1b. This distinct binding
behavior corroborates the conclusion that there are independent
contacts on RhoA for the HR1aPRK1 and HR1bPRK1
motifs.
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