Retinoic Acid Regulated Nuclear Matrix Associated Protein (RAMP)

RAMP is rich in serines, threonines, and basic residues. It has 2 WD repeats, a putative leucine zipper, a nuclear localization signal, a putative SH3-binding motif, 5 potential glycosylation sites, and several potential phosphorylation sites. In vitro translation resulted in an 85-kD RAMP protein.

RAMP mRNA and protein levels decreased in NT2 cells following RA treatment. RAMP translocated from the interphase nucleus to the metaphase cytoplasm during mitosis. During late-stage cytokinesis, RAMP concentrated at the midzone of dividing daughter cells. RAMP mRNA levels showed a positive correlation with the rate of cell proliferation, and overexpression of RAMP in NT2 cells induced a transient increase in proliferation.