TY  - JOUR
A1  - Meurer, Sabine
A1  - Pioch, Sylke
A1  - Wagner, Kristina
A1  - Müller-Esterl, Werner
A1  - Groß, Steffen
T1  - AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase
T2  - Journal of biological chemistry
N2  - Nitric oxide (NO)-sensitive soluble guanylyl cyclase (sGC) is the major cytosolic receptor for NO, catalyzing the conversion of GTP to cGMP. In a search for proteins specifically interacting with human sGC, we have identified the multidomain protein AGAP1, the prototype of an ArfGAP protein with a GTPase-like domain, Ankyrin repeats, and a pleckstrin homology domain. AGAP1 binds through its carboxyl terminal portion to both the α1 and β1 subunits of sGC. We demonstrate that AGAP1 mRNA and protein are co-expressed with sGC in human, murine, and rat cells and tissues and that the two proteins interact in vitro and in vivo. We also show that AGAP1 is prone to tyrosine phosphorylation by Src-like kinases and that tyrosine phosphorylation potently increases the interaction between AGAP1 and sGC, indicating that complex formation is modulated by reversible phosphorylation. Our findings may hint to a potential role of AGAP1 in integrating signals from Arf, NO/cGMP, and tyrosine kinase signaling pathways.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76144
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-761449
SN  - 0021-9258
VL  - 279.2004
IS  - 47
SP  - 49346
EP  - 49354
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -