Glucocorticoid receptor phosphorylation in mouse L-cells
dc.contributor.author | Sanchez, Edwin R. | en_US |
dc.contributor.author | Tienrungroj, Wilai | en_US |
dc.contributor.author | Dalman, Friedrich C. | en_US |
dc.contributor.author | Lin, Alexander L. -Y. | en_US |
dc.date.accessioned | 2006-04-07T20:01:08Z | |
dc.date.available | 2006-04-07T20:01:08Z | |
dc.date.issued | 1987 | en_US |
dc.identifier.citation | Sanchez, Edwin R., Tienrungroj, Wilai, Dalman, Friedrich C., Lin, Alexander L. -Y. (1987)."Glucocorticoid receptor phosphorylation in mouse L-cells." Journal of Steroid Biochemistry 27(1-3): 215-225. <http://hdl.handle.net/2027.42/26917> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GT-47FX6BX-G0/2/0549a647dd548037b29fa029792c2101 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/26917 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3320532&dopt=citation | en_US |
dc.description.abstract | This paper summarizes our observations on the phosphorylation state of untransformed and transformed glucocorticoid receptors isolated from 32P-labeled L-cells. The 300-350-kDa 9S untransformed murine glucocorticoid receptor complex is composed of a 100-kDa steroid-binding phosphoprotein and one or possibly two units of the 90-kDa heat shock protein (hsp90), which is also a phosphoprotein. Transformation of this complex to the 4S DNA-binding state is accompanied by dissociation of hsp90. When receptors in cytosol are transformed by heating at 25[deg]C, there is no gross change in the degree of phosphorylation of the steroid-binding protein. Both receptors that are bound to DNA after transformation under cell-free conditions and receptors that are located in the nucleus of cells incubated at 37[deg]C in the presence of glucocorticoid are labeled with 32P. The results of experiments in which the 32P-labeled receptor was submitted to limited proteolysis suggest that the 16-kDa DNA-binding domain is phosphorylated and that the 28-kDa steroid-binding domain is not. | en_US |
dc.format.extent | 1033508 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 | Glucocorticoid receptor phosphorylation in mouse L-cells | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pharmacology, The University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Pharmacology, The University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Pharmacology, The University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Pharmacology, The University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.identifier.pmid | 3320532 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/26917/1/0000483.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0022-4731(87)90313-X | en_US |
dc.identifier.source | Journal of Steroid Biochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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