High impact information on M-RIP

• M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells [1].
• These data support the importance of myosin phosphatase-Rho interacting protein-dependent targeting of myosin phosphatase to stress fibers for regulating myosin light chain phosphorylation state and morphology in human vascular smooth muscle cells [1].
• The gene silencing of p116Rip consistently and significantly increased myosin phosphorylation as well as stress fiber formation in cells [2].
• We used RNA interference to silence the expression of myosin phosphatase-Rho interacting protein in human vascular smooth muscle cells [1].
• Furthermore, myosin phosphatase-Rho interacting protein silencing resulted in marked phenotypic changes in vascular smooth muscle cells, including increased numbers of stress fibers, increased cell area, and reduced stress fiber inhibition in response to a Rho-kinase inhibitor [1].

Biological context of M-RIP

• Expressional cloning indicated the antigen against HFB-16 to be human KIAA0864 protein, which is supposed to be an alternative splicing product of p116Rip, whose function has not yet been elucidated [3].

Anatomical context of M-RIP

• Myosin phosphatase-Rho interacting protein silencing reduced the localization of the myosin binding subunit to stress fibers [1].
• p116Rip targets myosin phosphatase to the actin cytoskeleton and is essential for RhoA/ROCK-regulated neuritogenesis [4].
• A novel marker for Purkinje cells, KIAA0864 protein. An analysis based on a monoclonal antibody HFB-16 in developing human cerebellum [3].
• Using normal and abnormal human fetal hearts and cultured normal human fetal cardiomyocytes, we show that congenital cardiovascular malformations are associated with the overexpression of hRIP3, and evidence is found for a certain association between overexpression of hRIP3 and homocysteine-induced congenital cardiovascular malformations [5].

Associations of M-RIP with chemical compounds

• This reduction in stress fiber myosin phosphatase-Rho interacting protein and myosin binding subunit increased basal and lysophosphatidic acid-stimulated myosin light chain phosphorylation [1].
• Homocysteine, hRIP3 and congenital cardiovascular malformations [5].

Physical interactions of M-RIP

• An adjacent domain of M-RIP directly binds RhoA in a nucleotide-independent manner [6].

References