PMID- 32033037 OWN - NLM STAT- MEDLINE DCOM- 20201117 LR - 20201117 IS - 1422-0067 (Electronic) IS - 1422-0067 (Linking) VI - 21 IP - 3 DP - 2020 Feb 4 TI - Calmodulin-Binding Proteins in Muscle: A Minireview on Nuclear Receptor Interacting Protein, Neurogranin, and Growth-Associated Protein 43. LID - 10.3390/ijms21031016 [doi] LID - 1016 AB - Calmodulin (CaM) is an important Ca(2+)-sensing protein with numerous downstream targets that are either CaM-dependant or CaM-regulated. In muscle, CaM-dependent proteins, which are critical regulators of dynamic Ca(2+) handling and contractility, include calcineurin (CaN), CaM-dependant kinase II (CaMKII), ryanodine receptor (RyR), and dihydropyridine receptor (DHPR). CaM-regulated targets include genes associated with oxidative metabolism, muscle plasticity, and repair. Despite its importance in muscle, the regulation of CaM-particularly its availability to bind to and activate downstream targets-is an emerging area of research. In this minireview, we discuss recent studies revealing the importance of small IQ motif proteins that bind to CaM to either facilitate (nuclear receptor interacting protein; NRIP) its activation of downstream targets, or sequester (neurogranin, Ng; and growth-associated protein 43, GAP43) CaM away from their downstream targets. Specifically, we discuss recent studies that have begun uncovering the physiological roles of NRIP, Ng, and GAP43 in skeletal and cardiac muscle, thereby highlighting the importance of endogenously expressed CaM-binding proteins and their regulation of CaM in muscle. FAU - Moradi, Fereshteh AU - Moradi F AD - Department of Biological Sciences, Brock University, St. Catharines, ON L2S 3A1, Canada. FAU - Copeland, Emily N AU - Copeland EN AD - Centre for Neuroscience, Brock University, St. Catharines, ON L2S 3A1, Canada. AD - Centre for Bone and Muscle Health, Brock University, St. Catharines, ON L2S 3A1, Canada. FAU - Baranowski, Ryan W AU - Baranowski RW AD - Centre for Bone and Muscle Health, Brock University, St. Catharines, ON L2S 3A1, Canada. AD - Department of Kinesiology, Brock University, St. Catharines, ON L2S 3A1, Canada. FAU - Scholey, Aiden E AU - Scholey AE AD - Department of Kinesiology, Brock University, St. Catharines, ON L2S 3A1, Canada. FAU - Stuart, Jeffrey A AU - Stuart JA AUID- ORCID: 0000-0001-5894-0300 AD - Department of Biological Sciences, Brock University, St. Catharines, ON L2S 3A1, Canada. FAU - Fajardo, Val A AU - Fajardo VA AUID- ORCID: 0000-0003-4500-3347 AD - Centre for Neuroscience, Brock University, St. Catharines, ON L2S 3A1, Canada. AD - Centre for Bone and Muscle Health, Brock University, St. Catharines, ON L2S 3A1, Canada. AD - Department of Kinesiology, Brock University, St. Catharines, ON L2S 3A1, Canada. LA - eng GR - RGPIN 2019-05833/Natural Sciences and Engineering Research Council of Canada/ PT - Journal Article PT - Review DEP - 20200204 PL - Switzerland TA - Int J Mol Sci JT - International journal of molecular sciences JID - 101092791 RN - 0 (Calmodulin) RN - 0 (GAP-43 Protein) RN - 0 (Nuclear Receptor Interacting Protein 1) RN - 132654-77-4 (Neurogranin) RN - SY7Q814VUP (Calcium) SB - IM MH - Animals MH - Calcium/metabolism MH - Calcium Signaling/*physiology MH - Calmodulin/*metabolism MH - GAP-43 Protein/*metabolism MH - Humans MH - Muscle, Skeletal/metabolism MH - Myocardium/metabolism MH - Neurogranin/*metabolism MH - Nuclear Receptor Interacting Protein 1/*metabolism PMC - PMC7038096 OTO - NOTNLM OT - CaMKII OT - GAP43 OT - IQ-motif OT - NRIP OT - calcineurin OT - neurogranin OT - neuromodulin COIS- The authors declare no conflict of interest. EDAT- 2020/02/09 06:00 MHDA- 2020/11/18 06:00 PMCR- 2020/02/01 CRDT- 2020/02/09 06:00 PHST- 2019/12/16 00:00 [received] PHST- 2020/01/27 00:00 [revised] PHST- 2020/01/31 00:00 [accepted] PHST- 2020/02/09 06:00 [entrez] PHST- 2020/02/09 06:00 [pubmed] PHST- 2020/11/18 06:00 [medline] PHST- 2020/02/01 00:00 [pmc-release] AID - ijms21031016 [pii] AID - ijms-21-01016 [pii] AID - 10.3390/ijms21031016 [doi] PST - epublish SO - Int J Mol Sci. 2020 Feb 4;21(3):1016. doi: 10.3390/ijms21031016.