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Species-specific regulation of necroptosis by STK38-dependent RIPK1 phosphorylation

ABSTRACT: we identify serine/threonine kinase 38 (STK38) as a novel direct RIPK1 activator. STK38 binds to RIPK1, integrates into RIPK1-containing death complexes, and promotes RIPK1-dependent cell death.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Seongmi Kim

LAB HEAD: Jaewhan Song

PROVIDER: PXD066201 | Pride | 2026-07-10

REPOSITORIES: Pride

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	HJ_20170525_JMH_phospho04_add.raw	Raw
	HJ_20170525_JMH_phospho04_add_Human.xlsx	Xlsx
	HJ_20170525_JMH_phospho04_add_Human_addpeptide.xlsx	Xlsx
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Publications

Species-specific regulation of necroptosis by STK38-dependent RIPK1 phosphorylation.

Kim Seongmi S Lee Seung Ri SR Rho Hyunjin H Kim Hye-Jung HJ Ko Hyuk Wan HW Shin Donghyuk D Hong Seung-Mo SM Kim Minjoong M Yu Jiyoung J Kim Kyunggon K Chung Joon-Yong JY Song Jaewhan J

Cell death and differentiation 20260701

Receptor-interacting protein kinase 1 (RIPK1) is a key stress sensor regulating cell death, inflammation, and tumorigenesis, yet how RIPK1 becomes activated remains unclear. Here, we identify serine/threonine kinase 38 (STK38) as a novel direct RIPK1 activator. STK38 binds to RIPK1, integrates into RIPK1-containing death complexes, and accelerates RIPK1-dependent cell death. STK38 deletion suppresses RIPK1-mediated necroptosis and apoptosis. Moreover, TNF-α stimulation triggers MEKK2-dependent S ...[more]

PMID: 42387067

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