Localization of paxillin, a focal adhesion protein, to smooth muscle dense plaques, and the myotendinous and neuromuscular junctions of skeletal muscle.
In this report we have demonstrated that paxillin, a cytoskeletal protein which is present in focal adhesions, localizes in vivo to regions of cell-extracellular matrix interaction which are believed to be analogous to focal adhesions. Specifically, it is enriched in the dense plaques of chicken gizzard smooth muscle tissue and in the myotendinous junctions formed in Xenopus laevis tadpole tail skeletal muscle. In addition, paxillin was identified at the rat diaphragm neuromuscular junction. The distribution of paxillin is thus comparable to that of other focal adhesion proteins, for example, talin and vinculin, in these structures.
Turner
C E
CE
Department of Cell Biology and Anatomy, University of North Carolina, Chapel Hill 27599-7090.
Kramarcy
N
N
Sealock
R
R
Burridge
K
K
D000818:Animals; D000911:Antibodies, Monoclonal; D002448:Cell Adhesion / Q000502:physiology; D002645:Chickens; D003598:Cytoskeletal Proteins / Q000032:analysis; D005109:Extracellular Matrix / Q000378:metabolism; D008565:Membrane Proteins / Q000032:analysis*; D009124:Muscle Proteins / Q000032:analysis*; D009130:Muscle, Smooth / Q000737:chemistry*; D009132:Muscles / Q000737:chemistry*; D009469:Neuromuscular Junction / Q000737:chemistry*; D016608:Talin; D013710:Tendons / Q000737:chemistry; D014982:Xenopus laevis
D000911:Antibodies, Monoclonal; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009124:Muscle Proteins; D016608:Talin