PXD011764

PXD011764 is an original dataset announced via ProteomeXchange.

Title	N-myristoylation by NMT1 is POTEE-dependent to stimulate liver tumorigenesis via differentially regulating ubiquitination of targets
Description	Here, N-myristolyation, one kind post-translational modification, and its enzyme NMT1 but not NMT2, were found to be critical in liver cancer. Two categories of proteins, i.e. N-myristolyation down-regulated (NDP) and up-regulated protein (NUP) were revealed negatively and positively regulated by NMT1, respectively. Both NDP and NUP could be N-myristolyated by NMT1 indispensible of POTEE. However, N-myristolyation decreased and increased stability of NDP and NUP, respectively. NDP-specific binding protein RPL7A facilitated HISTIH4H, which has ubiquitin E3 ligase function, to ubiquitinate NDP. By contrast, NUP-specific binding protein HBB prevented NUP from ubiquitination by HISTIH4H. Notably, function of RPL7A and HBB were all NMT1-dependent. Moreover, NDP suppressed while NUP stimulated transformative phenotypes. Clinically, higher levels of NMT1 and NUP with lower levels of NDP had worse prognostic outcome. Collectively, N-myristolyation by NMT1 suppresses anti-tumorigenic NDP, whereas stimulates pro-tumorigenic NUP by interfering their ubiquitination to finally result in a pro-tumorigenic outcome in liver cancer.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:25:33.260.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Rachel Green
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2018-11-20 05:28:44	ID requested
1	2021-09-08 07:53:52	announced
⏵ 2	2024-10-22 05:25:34	announced	2024-10-22: Updated project metadata.

10.3389/fonc.2021.681366;

Zhu G, Wang F, Li H, Zhang X, Wu Q, Liu Y, Qian M, Guo S, Yang Y, Xue X, Sun F, Qiao Y, Pan Q, Differentially Regulating Ubiquitination of Targets. Front Oncol, 11():681366(2021) [pubmed]

submitter keyword: N-myristoylation by NMT1 is POTEE-dependent to stimulate liver tumorigenesis via differentially regulating ubiquitination of targets

Jiayi Wang
contact affiliation	Department of Clinical Laboratory, Shanghai Tenth People’s Hospital of Tongji University, Shanghai, 200072, China
contact email	karajan2@163.com
lab head
Rachel Green
contact affiliation	PTM Biolabs Inc.
contact email	xuan_mao@ptm-biolab.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/09/PXD011764

PRIDE project URI

• PRIDE
  1. PXD011764
     1. Label: PRIDE project
     2. Name: N-myristoylation by NMT1 is POTEE-dependent to stimulate liver tumorigenesis via differentially regulating ubiquitination of targets