Rack 1

The primary antibodies used were as follows: MEF2D (BD Biosciences, San Jose, CA, USA); MEF2A (C‐21 Santa Cruz Biotechnology, Dallas, TX, USA); p53 and pERK (Cell Signaling Technology, Leiden, the Netherlands); p21, Actin, anti‐BrdU, FLAG M2 and RACK‐1 (Sigma‐Aldrich); RAS (Abcam, Cambridge, MA, USA); GFP and HDAC4 (Paroni et al., 2004); and HDAC5 (Clocchiatti et al., 2015). Anti‐CD44‐FITC (BD Biosciences) and CD24‐APC (BioLegend, San Diego, CA, USA) were used with matched control antibodies, anti‐mouse IgG1 FITC and IgG2a APC (Miltenyi Biotec, Bergisch Gladbach, Germany). HDAC7 antibodies were generated in rabbits by injecting recombinant histidine‐tagged HDAC7 fragment aa 261–522. For anti‐HDAC7 antibody purification, HDAC7 was fused to glutathione S‐transferase and cross‐linked to glutathione‐Sepharose as described previously (Paroni et al., 2004).

It was performed as previously described (Wu et al., 2015 (link); Yang et al., 2019 (link)). Briefly, frozen sections were washed 10 min with 0.5% phosphate-buffered saline with Tween 20 (PBS-T) for three times and then blocked with 3% bovine serum albumin for 1 hr. After that, sections were incubated overnight at 4°C with the primary antibodies as follows: Calbindin (C9848, Sigma, 1:400), NeuN (MAB377, Millipore, 1:400), brain lipid binding protein (BLBP) (ab32423, Abcam, 1:500), Rack1 (R1905, Sigma, 1:400). The sections were washed 10 min with 0.5% PBS-T for three times again and subsequently subjected to Alexa Fluor-conjugated secondary antibodies (Biotium, 1:500). Nuclear staining was visualized with a mounting medium with 4′,6-diamidino-2-phenylindole (ZSGB-BIO). All images were taken from a laser scanning confocal microscope (Olympus FV1200) and then were processed and analyzed by FV10-ASW or Image Pro Plus 6.0 software.