Projects per year
Abstract
Membrane-bound guanylate cyclases (GCs)possessing intrinsic GC activity constitute a family of catalytically active membrane-associated proteins that play crucial roles in a myriad of signal transduction processes. Currently known membrane-bound GCs are catalytically monofunctional with a domain architecture that consists of an extracellular ligand-binding domain and an intracellular portion that is composed of an inactive kinase homology domain and a functional GC catalytic center. A novel class of GC-linked receptor kinases was unearthed using homology-guided bioinformatic data mining tools designed from annotated amino acid residues in the GC catalytic centers of lower eukaryotes. The GC catalytic center in this new class of membrane-bound GCs is encapsulated within an active kinase domain, thereby conferring a dual catalytic function to this class of proteins. This is contrary to currently known classical membrane-bound GCs, which are monofunctional. There are currently four members of this novel class of membrane-bound GCs which have been demonstrated to possess intrinsic GC and kinase activity. Although there is a paucity of information as to how the dual catalysis in bifunctional membrane-bound GCs is physiologically regulated, their mechanism of action maybe markedly distinct from that of classical membrane bound GCs.
Original language | English |
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Pages (from-to) | 1-13 |
Number of pages | 13 |
Journal | Springer Science Reviews |
Volume | 4 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2016 |
Keywords
- Guanylate cyclase activity
- Kinase activity
- Phosphorylation
- Signaling
- cGMP
Projects
- 1 Finished
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Molecular and cellular mechanisms of action of novel plant guanylyl cyclase enzymes - a new class of overlapping dual-domain molecules
Irving, H., Manallack, D. & Gehring, C.
Australian Research Council (ARC), Monash University
4/01/11 → 30/09/14
Project: Research