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

TY - JOUR

T1 - The calcium-sensor guanylate cyclase activating protein type 2 specific site in rod outer segment membrane guanylate cyclase type 1

AU - Duda, Teresa

AU - Fik-Rymarkiewicz, Ewa

AU - Venkataraman, Venkateswar

AU - Krishnan, Ramalingam

AU - Koch, Karl Wilhelm

AU - Sharma, Rameshwar K.

PY - 2005/5/17

Y1 - 2005/5/17

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/18544375013

UR - https://www.scopus.com/pages/publications/18544375013#tab=citedBy

U2 - 10.1021/bi050068x

DO - 10.1021/bi050068x

M3 - Article

C2 - 15882072

SN - 0006-2960

VL - 44

SP - 7336

EP - 7345

JO - Biochemistry

JF - Biochemistry

IS - 19

ER -