Erratum: The mTORC1 pathway stimulates glutamine metabolism and cell proliferation by repressing SIRT4 (A Conserved Dedicated Olfactory Circuit for Detecting Harmful Microbes in Drosophila (2012) 151(6) (1345–1357), (S0092867412013578), (10.1016/j.cell.2012.09.046))

(Cell 153, 840–854; May 9, 2013) Our paper reported that mTORC1 promotes glutamine consumption through the TCA cycle by activating glutamate dehydrogenase (GDH). After being contacted about apparent similarities between the streptavidin- and GDH-probed blots in Figure 2A, we determined that the data collection approach was not clearly described in the Experimental Procedures. Mono-ADP ribosylated GDH was detected first and the nitrocellulose membrane was then probed with streptavidin. The authors apologize for any confusion; the Experimental Methods subsection “ADP-Ribosylation Assay” should have been as follows: “Mono-ADP-ribosylation levels were determined as previously described (Mao et al., 2011) with slight modifications. DLD-1 cells stably expressing either SIRT4-HA or empty vector (EV) were transfected with 6-Biotin-NAD+ (Lonza transfection protocol). Twenty-four hours after transfection, cells were treated with rapamycin for 24 hr and harvested with IP buffer. Mitochondria were purified using the isolation kit from Pierce. Poly-ADP ribosylated proteins from mitochondrial samples were cleared using PAR antibody (1:200) with protein A beads for 1 hr. Avidin coated beads (1:10) (Sigma) were added and incubated for 1 hr at 4C. Samples were run in SDS-PAGE gels and proteins were transferred into nitrocellulose membranes. Mono-ADP ribosylated GDH was detected using the GDH antibody (Abcam). Following GDH detection, the membrane was incubated with Streptavidin-HRP (Abcam) to evaluate the levels of avidin control. Lysates to measure endogenous GDH and HA-SIRT4 over-expression were run in parallel.”