PDZ Protein In subject area:Pharmacology, Toxicology and Pharmaceutical Science ZASP (Z-band alternatively spliced PDZ-domain-containing protein) encodes a Z-disc-associated protein with a single N-terminal PDZ domain and three C-terminal LIM domains that mediate protein–protein interactions....
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This interaction has been further confirmed by immunohistochemical studies that demonstrated co-localization of Cypher and α-actinin at the Z-lines of cardiac muscle. We have also found that Cypher1 binds to protein kinase C through its LIM domains. Phosphorylation of Cypher by protein kinase C ...
D., Evans, S., and Chen, J. (2001). Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy. J. Cell Biol. 155, 605- 612.Zhou, Q., Chu, P.H., Huang, C., Cheng, C.F., Martone, M.E., Knoll, G., Shelton, G.D., Evans, S...
PDZ domains are abundant protein interaction modules that often recognize short amino acid motifs at the C-termini of target proteins. They regulate multiple biological processes such as transport, ion channel signaling, and other signal transduction sys
These proteins contain one N-terminal PDZ domain followed either by one C-terminal LIM domain (ALP subfamily; ALP, RIL, CLP-36) or three C-terminal LIM domains (Enigma subfamily; Enigma, ENH, ZASP/Cypher1) (Ref. [1], and therein). It has been suggested that PDZ-LIM proteins act as...
and in cells that OspE proteins interact with PDLIM7, a member of the PDLIM family of proteins, which contain a PDZ domain and one or more LIM domains, protein interaction domains that participate in a wide variety of functions, including activation of isoforms of protein kinase C (PKC). ...
PDZ (postsynaptic density protein-95/discs large/zonula occludens-1) domains are among the most common protein–protein interaction modules in multi-cellular organisms. They are involved in a variety of cellular processes including establishment and maintenance of cell polarity [8]. PDZ domains are ...
A combination of in vitro binding and yeast two-hybrid assays unexpectedly showed that PDZ domains derived from PSD95 bind both the C- and N-termini of the channels with comparable avidity. From doubly transfected HEK293 cells, Kv1.5 was found to co-immunoprecipitate with the PDZ protein, ...
“Actinin-associated LIM Protein: Identification of a Domain Interaction between PDZ and Spectrin-like Repeat Motifs”, The Journal of Cell Biology, Oct. 1997, pp. 507-515, vol. 139, No. 2. Yanagisawa, J., et al., “The Molecular interaction of Fas and FAP-1. A tripeptide blocker ...