Spartin recruits PKC-ζ via the PKC-ζ-interacting proteins ZIP1 and ZIP3 to lipid droplets
作者： Andreas Urbanczyk , Ralf Enz
DOI: 10.1111/J.1471-4159.2011.07367.X
关键词:
摘要: J. Neurochem. (2011) 118, 737–748. Abstract Protein kinase C-ζ interacting proteins (ZIP1-3) recruit the enzymatic activity of atypical protein C isoforms PKC-λ/ι or PKC-ζ to target proteins. In this study, we searched for binding partners ZIP3 in CNS and identified spartin, a multifunctional that is mutated spastic paraplegia type 20. transfected cells, spartin was present on surface lipid droplets (LD), whereas ZIP appeared intracellular speckles. presence ZIP1 were translocated spartin-positive LD. This translocation mediated by amino acids 196–393 interacted with an N-terminal region Furthermore, simultaneously PKC-ζ, resulting enrichment spartin/ZIP-labelled Without neither nor detected Interestingly, spartin/ZIP/PKC-ζ complex increased LD size. effect most pronounced upon incorporation isoform into trimer. Finally, co-localized axon terminals neurons mammalian retina. summary, describe as new partner ZIP/PKC-ζ dimer recruits show expressed regulates
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