Subcellular localization of LIM domain proteins in chicken retina

BEJARANO, C.A.; PAGANELLI, ALEJANDRA R.; RIOS, H.

Congreso; XXVII Congreso Anual de la Sociedad Argentina de Investigación en Neurociencias; 2012

CLP36 (PDLIM 1-3) is a protein member of the PDZ-LIM family that has 4functional domains:a PDZ domain at the N-terminal,1-3 LIM domains at the Cterminal which interacts to the actin cytoskeleton; aZASP-like domain that interacts with
-actinin(an actin-crosslinking protein) and ALP-like domain that interacts with protein kinases. It is known that the signaling pathway PDZ-LIM family proteins involve only the LIM domain and that PDZ domain is related to the anchored properties of this protein. There is little information about the role of CLP36 in central nervous systemand retina. The present study describes the immunohistochemistry localization of CLP36 in the chick retina and also we analyzed subcellular fractionation by western blot. Using an antibody which detects CLP36 we have observed that only the synaptic endings of double cones are stained. Subcellular fractionation showed that CLP36 is present at the 0.9M fraction (synaptosomes). Results allowed us to argue that CLP36could serveas a scaffoldof molecular complex and could be involvedin thesynaptic structure, making functional organization with actin. Our observationsin chick retina rise new questions about the regulatory pathways of CLP36protein and its potential role in synaptic plasticity in chick retina. PIP00404.