title: The immunolocalization and divergent roles of phosducin and phosducin-like protein in the retina.
abstract: OBJECTIVE
  These investigations were undertaken to compare and contrast the roles of phosducin and phosducin-like protein in the retina.
  
  
  METHODS
  Phosducin and phosducin-like protein were compared in an in vitro assay measuring their inhibition of transducin binding to light-activated rhodopsin. The two proteins were localized within the retina by immunoblot analyses and immunocytochemistry using affinity-purified antibodies with high specificity for each of the two homologs. The sensitivity of phosducin-like protein to phosphorylation was probed using in vitro protein kinase reactions.
  
  
  RESULTS
  Phosducin and phosducin-like protein were found to have similar, though not identical, transducin inhibiting activity in vitro. These two proteins were found to be localized dissimilarly within the retina, with spatial overlap limited to the inner segments of the photoreceptors. Phosducin is found exclusively in photoreceptor cells, including the synaptic and nuclear layers, while phosducin-like protein is found throughout the inner retinal layers, most abundantly in the bipolar cells of the inner nuclear layer. Phosducin-like protein is not efficiently phosphorylated by the protein kinases tested, indicating that its regulation differs from that of phosducin.
  
  
  CONCLUSIONS
  It appears that phosducin and phosducin-like protein play distinct roles in the retina. While phosducin is likely to be important in feedback regulation of the visual signal, such as in light adaptation, phosducin-like protein probably has little if any function in the phototransduction cascade. Phosducin-like protein may have a role in regulating the processing of visual signals by the neural cells of the inner retina.
authors.affiliation: Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA. cdthulin@chemdept.byu.edu
authors.forename: C D
authors.initials: CD
authors.lastname: Thulin
authors.forename: K
authors.initials: K
authors.lastname: Howes
authors.forename: C D
authors.initials: CD
authors.lastname: Driscoll
authors.forename: J R
authors.initials: JR
authors.lastname: Savage
authors.forename: T A
authors.initials: TA
authors.lastname: Rand
authors.forename: W
authors.initials: W
authors.lastname: Baehr
authors.forename: B M
authors.initials: BM
authors.lastname: Willardson
mesh_terms: D000818:Animals; D000918:Antibody Specificity; D002352:Carrier Proteins / Q000276:immunology / Q000378:metabolism* / Q000494:pharmacology / Q000502:physiology*; D002417:Cattle; D005136:Eye Proteins / Q000276:immunology / Q000378:metabolism* / Q000502:physiology*; D020555:GTP-Binding Protein Regulators; D019204:GTP-Binding Proteins / Q000378:metabolism; D015151:Immunoblotting; D007150:Immunohistochemistry; D051379:Mice; D018832:Molecular Chaperones; D009419:Nerve Tissue Proteins / Q000276:immunology / Q000378:metabolism* / Q000494:pharmacology / Q000502:physiology*; D010750:Phosphoproteins / Q000276:immunology / Q000378:metabolism* / Q000502:physiology*; D010766:Phosphorylation; D011485:Protein Binding / Q000187:drug effects; D011493:Protein Kinase C / Q000378:metabolism; D012160:Retina / Q000201:enzymology / Q000378:metabolism*; D012243:Rhodopsin / Q000378:metabolism; D012374:Rod Cell Outer Segment / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D005136:Eye Proteins; D020555:GTP-Binding Protein Regulators; D018832:Molecular Chaperones; D009419:Nerve Tissue Proteins; C498319:Pdcl protein, mouse; D010750:Phosphoproteins; C065631:phosducin; D012243:Rhodopsin; D011493:Protein Kinase C; D019204:GTP-Binding Proteins