Disease relevance of pat-3

• Sterility caused by RNAi of pat-3 and ECM molecules was suppressed by increased IP(3) signaling [1].

High impact information on pat-3

• At least nine protein bands with relative molecular weights in the range observed for known integrin alpha subunits coprecipitate with beta pat-3, and at least three of these bands migrate in SDS-PAGE with increased mobility when reduced [2].
• Characterization of beta pat-3 heterodimers, a family of essential integrin receptors in C. elegans [2].
• Finally, immunocytochemical analysis revealed that beta pat-3 is expressed in the embryo and in many cell types postembryonically, including muscle, somatic gonad, and coelomocytes, suggesting multiple roles for integrin heterodimers containing this beta subunit in the developing animal [2].
• Contractile muscle cells showed disorganization of the actin cytoskeleton leading to complete paralysis, a phenotype that was also observed with depletion of pat-2 and pat-3 integrins [3].
• Either the dominant negative mutant pat-3 beta integrin or disruption of talin expression block ovulation [1].

Biological context of pat-3

• Role of beta pat-3 integrins in development and function of Caenorhabditis elegans muscles and gonads, suggesting that the interaction between the cell and the extracellular matrix (ECM) is also important for ovulation [1].

Analytical, diagnostic and therapeutic context of pat-3

• Immunoblot analysis using a polyclonal antiserum against the cytoplasmic domain showed that beta pat-3 migrates in SDS-PAGE with apparent M(r) of 109 k and 120 k under nonreducing and reducing conditions, respectively [2].
• Immunoprecipitations of beta pat-3 from developmentally staged populations of C. elegans showed that the expression of several of these bands changes during development [2].

References