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Structure and regulation of soluble guanylate cyclase.

Publication ,  Journal Article
Derbyshire, ER; Marletta, MA
Published in: Annual review of biochemistry
January 2012

Nitric oxide (NO) is an essential signaling molecule in biological systems. In mammals, the diatomic gas is critical to the cyclic guanosine monophosphate (cGMP) pathway as it functions as the primary activator of soluble guanylate cyclase (sGC). NO is synthesized from l-arginine and oxygen (O(2)) by the enzyme nitric oxide synthase (NOS). Once produced, NO rapidly diffuses across cell membranes and binds to the heme cofactor of sGC. sGC forms a stable complex with NO and carbon monoxide (CO), but not with O(2). The binding of NO to sGC leads to significant increases in cGMP levels. The second messenger then directly modulates phosphodiesterases (PDEs), ion-gated channels, or cGMP-dependent protein kinases to regulate physiological functions, including vasodilation, platelet aggregation, and neurotransmission. Many studies are focused on elucidating the molecular mechanism of sGC activation and deactivation with a goal of therapeutic intervention in diseases involving the NO/cGMP-signaling pathway. This review summarizes the current understanding of sGC structure and regulation as well as recent developments in NO signaling.

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Published In

Annual review of biochemistry

DOI

EISSN

1545-4509

ISSN

0066-4154

Publication Date

January 2012

Volume

81

Start / End Page

533 / 559

Related Subject Headings

  • Soluble Guanylyl Cyclase
  • Signal Transduction
  • Receptors, Cytoplasmic and Nuclear
  • Nitric Oxide
  • Isoenzymes
  • Humans
  • Guanylate Cyclase
  • Cyclic GMP
  • Biochemistry & Molecular Biology
  • Animals
 

Citation

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Derbyshire, E. R., & Marletta, M. A. (2012). Structure and regulation of soluble guanylate cyclase. Annual Review of Biochemistry, 81, 533–559. https://doi.org/10.1146/annurev-biochem-050410-100030
Derbyshire, Emily R., and Michael A. Marletta. “Structure and regulation of soluble guanylate cyclase.Annual Review of Biochemistry 81 (January 2012): 533–59. https://doi.org/10.1146/annurev-biochem-050410-100030.
Derbyshire ER, Marletta MA. Structure and regulation of soluble guanylate cyclase. Annual review of biochemistry. 2012 Jan;81:533–59.
Derbyshire, Emily R., and Michael A. Marletta. “Structure and regulation of soluble guanylate cyclase.Annual Review of Biochemistry, vol. 81, Jan. 2012, pp. 533–59. Epmc, doi:10.1146/annurev-biochem-050410-100030.
Derbyshire ER, Marletta MA. Structure and regulation of soluble guanylate cyclase. Annual review of biochemistry. 2012 Jan;81:533–559.

Published In

Annual review of biochemistry

DOI

EISSN

1545-4509

ISSN

0066-4154

Publication Date

January 2012

Volume

81

Start / End Page

533 / 559

Related Subject Headings

  • Soluble Guanylyl Cyclase
  • Signal Transduction
  • Receptors, Cytoplasmic and Nuclear
  • Nitric Oxide
  • Isoenzymes
  • Humans
  • Guanylate Cyclase
  • Cyclic GMP
  • Biochemistry & Molecular Biology
  • Animals