Analysis of DHHC Acyltransferases Implies Overlapping Substrate Specificity and a Two-Step Reaction Mechanism

DC FieldValueLanguage
dc.contributor.authorHou, Haitong
dc.contributor.authorPeter, Arun T. John
dc.contributor.authorMeiringer, Christoph
dc.contributor.authorSubramanian, Kanagaraj
dc.contributor.authorUngermann, Christian
dc.date.accessioned2021-12-23T15:59:45Z-
dc.date.available2021-12-23T15:59:45Z-
dc.date.issued2009
dc.identifier.issn13989219
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/4121-
dc.description.abstractAsp-His-His-Cys (DHHC) cysteine-rich domain (CRD) acyltransferases are polytopic transmembrane proteins that are found along the endomembrane system of eukaryotic cells and mediate palmitoylation of peripheral and integral membrane proteins. Here, we address the in vivo substrate specificity of five of the seven DHHC acyltransferases for peripheral membrane proteins by an overexpression approach. For all analysed DHHC proteins we detect strongly overlapping substrate specificity. In addition, we now show acyltransferase activity for Pfa5. More importantly, the DHHC protein Pfa3 is able to trap several substrates at the vacuole. For Pfa3 and its substrate Vac8, we can distinguish two consecutive steps in the acylation reaction: an initial binding that occurs independently of its central cysteine in the DHHC box, but requires myristoylation of its substrate Vac8, and a DHHC-motif dependent acylation. Our data also suggest that proteins can be palmitoylated on several organelles. Thus, the intracellular distribution of DHHC proteins provides an acyltransferase network, which may promote dynamic membrane association of substrate proteins.
dc.description.sponsorshipHans-Muhlenhoff foundation; Boehringer Ingelheims FondsBoehringer Ingelheim; [SFB431]; We thank Nicolas Davis for yeast strains, Angela Perz for experimental support, Clemens Ostrowicz for comments and all members of the Ungermann lab for fruitful discussions. This work was supported by the SFB431. C. U. is supported by the Hans-Muhlenhoff foundation. A. T. JP was supported by a mobility fellowship of the Boehringer Ingelheims Fonds.
dc.language.isoen
dc.publisherWILEY
dc.relation.ispartofTRAFFIC
dc.subjectacyltransferase
dc.subjectCell Biology
dc.subjectDHHC
dc.subjectDOMAIN
dc.subjectLOCALIZATION
dc.subjectNITRIC-OXIDE SYNTHASE
dc.subjectpalmitoylation
dc.subjectPALMITOYLTRANSFERASES
dc.subjectPfa3
dc.subjectPLASMA-MEMBRANE
dc.subjectPROTEIN PALMITOYLATION
dc.subjectSACCHAROMYCES-CEREVISIAE
dc.subjectVac8
dc.subjectVAC8P
dc.subjectVACUOLE
dc.subjectYEAST
dc.titleAnalysis of DHHC Acyltransferases Implies Overlapping Substrate Specificity and a Two-Step Reaction Mechanism
dc.typejournal article
dc.identifier.doi10.1111/j.1600-0854.2009.00925.x
dc.identifier.isiISI:000267714900010
dc.description.volume10
dc.description.issue8
dc.description.startpage1061
dc.description.endpage1073
dc.contributor.orcid0000-0001-8356-5469
dc.contributor.orcid0000-0003-4493-9645
dc.contributor.researcheridE-8416-2013
dc.contributor.researcheridD-5188-2019
dc.identifier.eissn16000854
dc.publisher.place111 RIVER ST, HOBOKEN 07030-5774, NJ USA
dcterms.isPartOf.abbreviationTraffic
crisitem.author.netidUnCh999-
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