Calcium and calmodulin inhibit phosphorylation of a novel auditory nerve protein
dc.contributor.author | Coling, Donald E. | en_US |
dc.contributor.author | Naik, Rajiv M. | en_US |
dc.contributor.author | Schacht, Jochen | en_US |
dc.date.accessioned | 2006-04-10T18:27:40Z | |
dc.date.available | 2006-04-10T18:27:40Z | |
dc.date.issued | 1994-01 | en_US |
dc.identifier.citation | Coling, Donald E., Naik, Rajiv M., Schacht, Jochen (1994/01)."Calcium and calmodulin inhibit phosphorylation of a novel auditory nerve protein." Hearing Research 72(1-2): 197-205. <http://hdl.handle.net/2027.42/31903> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T73-487CV6V-4N/2/681183783b8d44166bbae2de8962ab35 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/31903 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7512086&dopt=citation | en_US |
dc.description.abstract | The growing use of cochlear prosthetic devices and demonstrations of direct ototoxic insult to spiral ganglion neurons make it imperative to gain an understanding of intracellular biochemical regulation in primary sensory neurons. Calcium and calmodulin regulate many aspects of neuronal cellular physiology through stimulation of protein kinase activity. We have previously demonstrated the presence of calmodulin-dependent protein kinase substrates in the guinea pig modiolus and, additionally, the presence of two proteins (12 kDa and 81 kDa, designated as pl2 and p81) whose phosphorylation is blocked by calcium and calmodulin (Coling and Schacht, 1991). Here, we investigate three models for this unusual regulatory mechanism. The effects of calcium, calmodulin and trifluoperazine on dephosphorylation of both proteins suggests that calmodulin inhibits protein kinase activity. P81 was identified by immunoprecipitation as the myristoylated alanine-rich C kinase substrate (MARCKS), a ubiquitous actin-binding protein. Two observations indicate that MARCKS may be regulated differently in acoustic nerve than in cerebral cortex. 32P incorporation was significantly higher in acoustic nerve than in brain. The calmodulin-dependent block of MARCKS phosphorylation was observed only in acoustic nerve. p12 shares several characteristics with myelin basic protein (MBP). We used a double label assay with 32P autoradiography and immunoblotting to show that p12 is in fact distinct from MBP. We suggest that either p12 or p12 kinase may be either specific to the peripheral auditory system or novel marker proteins for that tissue. | en_US |
dc.format.extent | 1298622 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Calcium and calmodulin inhibit phosphorylation of a novel auditory nerve protein | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Kresge Hearing Research Institute, University of Michigan, Ann Arbor, MI, USA. | en_US |
dc.contributor.affiliationum | Kresge Hearing Research Institute, University of Michigan, Ann Arbor, MI, USA. | en_US |
dc.contributor.affiliationum | Kresge Hearing Research Institute, University of Michigan, Ann Arbor, MI, USA. | en_US |
dc.identifier.pmid | 7512086 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/31903/1/0000856.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0378-5955(94)90219-4 | en_US |
dc.identifier.source | Hearing Research | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.