N-terminal residues regulate proteasomal degradation of AANAT
dc.contributor.author | Huang, Zheping | en_US |
dc.contributor.author | Liu, Tiecheng | en_US |
dc.contributor.author | Borjigin, Jimo | en_US |
dc.date.accessioned | 2011-01-31T17:49:55Z | |
dc.date.available | 2011-06-09T15:09:40Z | en_US |
dc.date.issued | 2010-04 | en_US |
dc.identifier.citation | Huang, Zheping; Liu, Tiecheng; Borjigin, Jimo; (2010). "N-terminal residues regulate proteasomal degradation of AANAT." Journal of Pineal Research 48(3): 290-296. <http://hdl.handle.net/2027.42/79290> | en_US |
dc.identifier.issn | 0742-3098 | en_US |
dc.identifier.issn | 1600-079X | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/79290 | |
dc.description.abstract | Serotonin N -acetyltransferase (AANAT) catalyzes the conversion of serotonin to N -acetylserotonin, which is the immediate precursor for formation of melatonin. Although it is known that AANAT is degraded via the proteasomal proteolysis, detailed mechanisms are not defined. In this paper, we tested the in vivo role of proteasome inhibition on AANAT activity and melatonin release and examined the amino acid residues in AANAT that contribute to the proteasome degradation. We have shown that inhibition of proteasome activities in vivo in the intact pineal gland fails to prevent the light-induced suppression of melatonin secretion. Furthermore, in cell lines stably expressing AANAT, inhibition of proteasomal proteolysis, which resulted in a large accumulation of AANAT protein, similarly failed to increase AANAT enzyme activity proportional to the amount of proteins accumulated. Site-directed mutagenesis analysis of AANAT revealed that the AANAT degradation is independent of lysine and the two surface cysteine residues. Deletion analysis of N-terminus identified the second amino acid leucine (L2) as the key residue that contributes to the proteasomal proteolysis of AANAT protein. These results suggest that rat AANAT protein is degraded via the N-end rule pathway of proteasomal proteolysis and the leucine at the N-terminus appears to be the key residue recognized by N-end rule pathway. | en_US |
dc.format.extent | 710273 bytes | |
dc.format.extent | 3106 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.subject.other | AANAT | en_US |
dc.subject.other | Melatonin | en_US |
dc.subject.other | Pineal Gland | en_US |
dc.subject.other | Proteasome | en_US |
dc.subject.other | Protein Degradation | en_US |
dc.title | N-terminal residues regulate proteasomal degradation of AANAT | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Internal Medicine and Specialties | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.identifier.pmid | 20210853 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/79290/1/j.1600-079X.2010.00753.x.pdf | |
dc.identifier.doi | 10.1111/j.1600-079X.2010.00753.x | en_US |
dc.identifier.source | Journal of Pineal 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.