Home > Authorities > Grants > Record #406950 > print

001     406950
005     20230212180951.0
024 7 _ |a G:(EU-Grant)772039
|d 772039
|2 CORDIS
024 7 _ |a G:(EU-Call)ERC-2017-COG
|d ERC-2017-COG
|2 CORDIS
024 7 _ |a corda__h2020::772039
|2 originalID
035 _ _ |a G:(EU-Grant)772039
150 _ _ |a Discovery and functional significance of post-translational N-terminal acetylation
|y 2018-06-01 - 2023-05-31
371 _ _ |a University of Bergen
|b University of Bergen
|d Norway
|e http://www.uib.no/en/node/36362
|v CORDIS
372 _ _ |a ERC-2017-COG
|s 2018-06-01
|t 2023-05-31
450 _ _ |a NterAct
|w d
|y 2018-06-01 - 2023-05-31
510 1 _ |0 I:(DE-588b)5098525-5
|a European Union
|2 CORDIS
680 _ _ |a In mammalian cells, N-terminal (Nt) acetylation is one of the most abundant protein modifications. It is catalysed by N-terminal acetyltransferases (NATs) and mostly occurs co-translationally. However, in contrast to the defined co-translational NATs, post-translational NATs which have crucial regulatory roles are mostly unexplored. Distinct peptide hormones regulate appetite, metabolism, sexual behaviour and pain, and their biological activity is critically modulated by post-translational Nt-acetylation. However, the identity of the NAT responsible for this modification, ‘HormNat’, is unknown, thus the molecular and physiological ramifications of this regulatory circuit remain elusive. Another example is actin, a key regulator of cell motility and cell division. The actin N-terminus is crucial for actin function and in mammals actin is modified by an unknown post-translational NAT, ‘ActNat’. Hence, the objectives of this project are to identify these human NATs acting post-translationally, and to investigate their molecular mechanisms, regulation and impact. We will identify the novel NATs by a combination of classical and newly developed in-house tools like in vitro acetylation assays, unique bisubstrate analogues, Nt-acetylation specific antibodies, and targeted mass spectrometry. Interestingly, Nt-acetylation is considered irreversible, but there is reason to believe that specific substrates are Nt-deacetylated. Elucidation of post-translational NATs and the reversible nature of Nt-acetylation would represent a new era in the field of protein and peptide regulation and identify key cellular and organismal switches.
909 C O |o oai:juser.fz-juelich.de:849425
|p authority:GRANT
|p authority
909 C O |o oai:juser.fz-juelich.de:849425
970 _ _ |a oai:dnet:corda__h2020::41ee4ea85aa7e6d3b9b0f55fc7a27004
980 _ _ |a G
980 _ _ |a CORDIS
980 _ _ |a AUTHORITY

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21