Cellular retinoic acid-binding protein 2 (CRABP2) is a cytosolic, lipid-binding protein thought to bind its natural ligand, all-trans-retinoic acid (atRA) and mediate its delivery to retinoic acid receptors (RARs) within the nucleus (Kleywegt et al. 1994). CRABP2 forms a beta-barrel structure within which a hydrophobic ligand can be accommodated. Once atRA binds to CRABP2, the resulting complex translocates to the nucleus (Budhu & Noy 2002). A ligand activated nuclear-localisation signal appears to be critical for nuclear localisation (Sessler & Noy 2005). Sumoylation of CRABPs is also essential for atRA-induced dissociation of CRABPs from the ER membrane. For CRABP2, the site K102 is sumoylated (Majumdar et al. 2011).
Kleywegt, GJ, Bergfors, T, Senn, H, Le Motte, P, Gsell, B, Shudo, K, Jones, TA
Budhu, AS, Noy, N
Majumdar, A, Petrescu, AD, Xiong, Y, Noy, N
Sessler, RJ, Noy, N
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