Author:
Cheng Christiana L.,Molday Robert S.
Abstract
In photoreceptors, the assembly of signaling molecules into macromolecular complexes is important for phototransduction and maintaining the structural integrity of rod outer segments (ROS). However, the molecular composition and formation of these complexes are poorly understood. Using immunoprecipitation and mass spectrometry, 4.1G was identified as a new interacting partner for the cyclic-nucleotide gated (CNG) channels in ROS. 4.1G is a widely expressed multifunctional protein that plays a role in the assembly and stability of membrane protein complexes. Multiple splice variants of 4.1G were cloned from bovine retina. A smaller splice variant of 4.1G selectively interacted with CNG channels not associated with peripherin-2-CNG channel complex. A combination of truncation studies and domain binding assays demonstrated that CNG channels selectively interacted with 4.1G through its FERM and CTD domains. By immunofluorescence, punctate labeling of 4.1G partially co-localized with CNG channels in the ROS. Our studies indicate that 4.1G interact with a subset of CNG channels in ROS and implicate this protein-protein interaction in organizing the spatial arrangement of CNG channels in the plasma membrane of outer segments.
Publisher
The Company of Biologists
Cited by
12 articles.
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