Fig. 7: The RRM domains of hnRNP L are critical for its role in oxaliplatin-induced DNA repair. | Cell Death & Disease

Fig. 7: The RRM domains of hnRNP L are critical for its role in oxaliplatin-induced DNA repair.

From: Heterogeneous nuclear ribonucleoprotein L facilitates recruitment of 53BP1 and BRCA1 at the DNA break sites induced by oxaliplatin in colorectal cancer

Fig. 7

a Immunoprecipitation of exogenous hnRNP L-FLAG by anti-FLAG antibody, with or without RNAse. Cofactors were examined by western blotting. b HnRNP L colocalizes with DNA repair factors in oxaliplatin-treated SW620 cells, as demonstrated by immunofluorescent colocalization with γ-H2AX, 53BP1, ATM, and BRCA1. Images in red represent the detection by a Texas-red-conjugated secondary antibody, whereas green represents FITC. Nuclei were visualized by 4 Ј, 6 Ј -diamino-2-phenylindole staining. Scale bar represents 10 μm. c Representation of the various hnRNP L mutants used in apoptosis complementation and immunoprecipitation experiments. The “Δ” with numbers indicates the specific RRM domain deleted. d Western blot analysis shows the protein expression and interaction associated with each of the LR constructs. e Representative fluorescence-activated cell sorter (FACS) data of apoptosis complementation experiments with different LR constructs. f Apoptosis data are shown as mean ± s.e.m. of quartic experiments. Statistical significance was evaluated by unpaired t test. *P < 0.05, ***P < 0.001, ns: no significant difference. g Model for the role of hnRNP L in DNA repair caused by oxaliplatin-induced DNA breaks: hnRNP L binds with 53BP1 or BRCA1 and is recruited to DNA damage sites following the phosphorylation of ATM and H2AX. 53BP1 or BRCA1 fails to recruit to or retain at the break sites after hnRNP L depletion

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