The calcium-sensor guanylate cyclase activating protein type 2 specific site in rod outer segment membrane guanylate cyclase type 1

Teresa Duda, Ewa Fik-Rymarkiewicz, Venkateswar Venkataraman, Ramalingam Krishnan, Karl Wilhelm Koch, Rameshwar K. Sharma

Research output: Contribution to journalArticle

38 Scopus citations

Abstract

The rod outer segment membrane guanylate cyclase type 1 (ROS-GC1), originally identified in the photoreceptor outer segments, is a member of the subfamily of Ca2+-modulated membrane guanylate cyclases. In phototransduction, its activity is tightly regulated by its two Ca 2+-sensor protein parts, GCAP1 and GCAP2. This study maps the GCAP2-modulatory site in ROS-GC1 through the use of multiple techniques involving surface plasmon resonance binding studies with soluble ROS-GC1 constructs, coimmunoprecipitation, functional reconstitution experiments with deletion mutants, and peptide competition assays. The findings show that the sequence motif of the core GCAP2-modulatory site is Y965-N981 of ROS-GC1. The site is distinct from the GCAP1-modulatory site. It, however, partially overlaps with the S100B-regulatory site. This indicates that the Y965-N981 motif tightly controls the Ca2+-dependent specificity of ROS-GC1. Identification of the site demonstrates an intriguing topographical feature of ROS-GC1. This is that the GCAP2 module transmits the Ca2+ signals to the catalytic domain from its C-terminal side and the GCAP1 module from the distant N-terminal side.

Original languageEnglish (US)
Pages (from-to)7336-7345
Number of pages10
JournalBiochemistry
Volume44
Issue number19
DOIs
StatePublished - May 17 2005

All Science Journal Classification (ASJC) codes

  • Biochemistry

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