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ProteomicsTEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts
Eukaryotic topoisomerase 1 (TOP1) regulates DNA topology to ensure efficient DNA replication and transcription. TOP1 is also a major driver of endogenous genome instability, particularly when its catalytic intermediate - a covalent TOP1-DNA adduct known as a TOP1 cleavage complex (TOP1cc) - is stabi...
ORGANISM(S): Homo sapiens (Human) 
2020-03-13 | PXD017239 | Pride
Protein-dna adducts Vcp/p97 Top1 Tex264 Dna repair Genome stability Sprtn Dna replication 
ProteomicsNucleophagy removes cytotoxic trapped PARP1
Poly (ADP-ribose) polymerase inhibitors (PARPi) induce cytotoxicity in homologous recombination repair (HRR)-deficient cancers by causing PARP1 to become trapped on chromatin, resulting in irreparable replication-associated DNA damage. Cancer cells commonly develop resistance to PARPi, with a recent...
ORGANISM(S): Homo sapiens (Human) 
2026-04-15 | PXD071389 | Pride
Hdx-ms 
UnknownTEX264 at the intersection of autophagy and DNA repair.
Not available
S-EPMC8865260 | biostudies-literature
UnknownTex264 Binding to SNX27 Regulates Itgα5 Receptor Membrane Recycling and Affects Cell Migration.
Not available
S-EPMC9274233 | biostudies-literature
UnknownTEX264 Is an Endoplasmic Reticulum-Resident ATG8-Interacting Protein Critical for ER Remodeling during Nutrient Stress.
Not available
S-EPMC6747008 | biostudies-literature
UnknownTEX264 is a major receptor for mammalian reticulophagy.
Not available
S-EPMC6735500 | biostudies-literature
UnknownTEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts.
Not available
S-EPMC7062751 | biostudies-literature
GenomicsTEX264 drives selective autophagy of DNA lesions to promote DNA repair and cell survival
TEX264 drives selective autophagy of DNA lesions to promote DNA repair and cell survival
PRJNA1013058 | ENA
UnknownPhosphorylation by casein kinase 2 enhances the interaction between ER-phagy receptor TEX264 and ATG8 proteins.
Not available
S-EPMC9171416 | biostudies-literature
UnknownWhen acidic residues do not mimic phosphorylation: high-affinity binding of the reticulophagy receptor TEX264 to LC3/GABARAP.
Not available
S-EPMC9629098 | biostudies-literature
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