PXD008942

PXD008942 is an original dataset announced via ProteomeXchange.

Title	Mass spectrometric evidence for neuropeptide-amidating enzymes in C. elegans
Description	Neuropeptides constitute a vast and functionally diverse family of neurochemical signaling molecules, and are widely involved in the regulation of various physiological processes. The nematode C. elegans is well-suited for the study of neuropeptide biochemistry and function, as neuropeptide biosynthesis enzymes are not essential for C. elegans viability. This permits the study of neuropeptide biosynthesis in mutants lacking certain neuropeptide-processing enzymes. Mass spectrometry has been used to study the effects of proprotein convertase and carboxypeptidase mutations on proteolytic processing of neuropeptide precursors and on the peptidome in C. elegans. However, the enzymes required for the last step in the production of many bioactive peptides – the carboxyterminal amidation reaction – have not been characterized in this manner. Here, we describe three genes that encode homologs of neuropeptide amidation enzymes in C. elegans and used tandem LC-MS to compare neuropeptides in wild-type animals with those in newly generated mutants for these putative amidation enzymes. We report that mutants lacking both a functional peptidylglycine α-hydroxylating monooxygenase (PHM) and a peptidylglycine α-amidating monooxygenase (PAM) had a severely altered neuropeptide profile and also a decreased number of offspring. Interestingly, single mutants of the amidation enzymes still expressed some fully processed amidated neuropeptides, indicating the existence of a redundant amidation mechanism in C. elegans. In summary, the key steps in neuropeptide-processing in C. elegans seem to be executed by redundant enzymes, and loss of these enzymes severely affects brood size, supporting the need of amidated peptides for C. elegans reproduction.
HostingRepository	PRIDE
AnnounceDate	2018-03-12
AnnouncementXML	Submission_2018-03-12_03:41:36.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD008942
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Sven Van Bael
SpeciesList	scientific name: Caenorhabditis elegans; NCBI TaxID: 6239;
ModificationList	Phospho; Amidated; Glu->pyro-Glu; Oxidation; Gln->pyro-Glu
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-02-13 01:57:54	ID requested
⏵ 1	2018-03-12 03:41:37	announced

Van Bael S, Watteyne J, Boonen K, De Haes W, Menschaert G, Ringstad N, Horvitz HR, Schoofs L, Husson SJ, Temmerman L, . J Biol Chem, 293(16):6052-6063(2018) [pubmed]

curator keyword: Biological

submitter keyword: Peptidomics

mass spectrometry

neuropeptide

amidation

copper monooxygenase

PHM

PAL

PAM

Caenorhabditis elegans

LC-orbitrap MS

Liesbet Temmerman
contact affiliation	Department of Biology KU Leuven (University of Leuven) Belgium
contact email	Liesbet.Temmerman@kuleuven.be
lab head
Sven Van Bael
contact affiliation	KU Leuven
contact email	sven.vanbael@kuleuven.be
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD008942
     1. Label: PRIDE project
     2. Name: Mass spectrometric evidence for neuropeptide-amidating enzymes in C. elegans