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Resources » Paper

Qadota H et al. (2000) Japanese Worm Meeting "Functional analysis of PKN-1, an effector of Rho GTPase, in C. elegans muscle"

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    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00011908

    Qadota H, & Kaibuchi K (2000). Functional analysis of PKN-1, an effector of Rho GTPase, in C. elegans muscle presented in Japanese Worm Meeting. Unpublished information; cite only with author permission.

    The Rho family GTPases (Rho, Rac, Cdc42) are involved in the regulation of actin reorganization, cell polarity, cell growth, and cell-cell adhesion. The Rho family GTPases have two interconvertible forms; the GTP-bound active and GDP-bound inactive forms. The GTP-bound form of Rho family GTPases interacts with their specific effectors. The GTP-bound form of RhoA binds preferentially to Protein Kinase N (PKN), Rho-kinase (also called ROK), myosin binding subunit of myosin phosphatase (MBS). Besides proceeding of functional analysis of Rho-kinase and MBS, the physiological functions of PKN remain to be clarified. Here we attempted to examine physiological functions of PKN using C. elegans as a genetic model system. Previously, we reported the identification of the C. elegans homologue of PKN, PKN-1, and its expression in the muscle cells (Qadota, et al., 12 th C. elegans meeting). To investigate effects of activated PKN-1, we expressed PKN-1 under the control of heat shock promoter. Overexpression of a catalytic domain of PKN-1 caused abnormal, loopy, movement of worms. Since the heat shock promoter can drive the expression of the downstream gene in all tissues, we next determined the tissues in which the catalytic domain of PKN-1 functions by two methods. First, mosaic analysis revealed that the expression of the catalytic domain of PKN-1 in neurons is dispensable for loopy movement and that the expression in all body wall muscle cells is required for loopy movement. Second, the expression of the catalytic domain of PKN-1 under the control of the body wall muscle specific promoter caused slightly loopy movement. These results suggest that the activation of PKN-1 in the muscle cells affects balance between contraction and relaxation in the C. elegans body wall muscle. Now we have a plan to examine a response of transgenic worms expressing the catalytic domain of PKN-1 to drugs to inhibit muscle excitation and will discuss the function of PKN-1 in the muscle cells from pharmacological results.


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