Dimerization activates the Inversin complex in .

Genetic, colocalization, and biochemical studies suggest that the ankyrin repeat-containing proteins Inversin (INVS) and ANKS6 function with the NEK8 kinase to control tissue patterning and maintain organ physiology. It is unknown whether these three proteins assemble into a static "Inversin complex" or one that adopts multiple bioactive forms. Through the characterization of hyperactive alleles in , we discovered that the Inversin complex is activated by dimerization.

Dimerization activates the Inversin complex in .

Genetic, colocalization, and biochemical studies suggest that the ankyrin repeat-containing proteins Inversin (INVS) and ANKS6 function with the NEK8 kinase to control tissue patterning and maintain organ physiology. It is unknown whether these three proteins assemble into a static "Inversin complex" or one that adopts multiple bioactive forms. Through characterization of hyperactive alleles in , we discovered that the Inversin complex is activated by dimerization.

The Caenorhabditis elegans ASPP homolog APE-1 is a junctional protein phosphatase 1 modulator.

How serine/threonine phosphatases are spatially and temporally tuned by regulatory subunits is a fundamental question in cell biology. Ankyrin repeat, SH3 domain, proline-rich-region-containing proteins are protein phosphatase 1 catalytic subunit binding partners associated with cardiocutaneous diseases. Ankyrin repeat, SH3 domain, proline-rich-region-containing proteins localize protein phosphatase 1 catalytic subunit to cell-cell junctions, but how ankyrin repeat, SH3 domain, proline-rich-region-containing proteins localize and whether they regulate protein phosphatase 1 catalytic subunit activity in vivo is unclear.

Oxidative stress differentially induces tau dissociation from neuronal microtubules in neurites of neurons cultured from different regions of the embryonic Gallus domesticus brain.

Abnormal phosphorylation of microtubule-associated proteins such as tau has been shown to play a role in neurodegenerative disorders. It is hypothesized that oxidative stress-induced aggregates of hyperphosphorylated tau could lead to the microtubule network degradation commonly associated with neurodegeneration. We investigated whether oxidative stress induced tau hyperphosphorylation and focused on neurite degradation using cultured neurons isolated from the embryonic chick brain as a model system.