Reactome | SUMO-CRABP2 dissociates from atRA:RAR:RXR

SUMO-CRABP2 dissociates from atRA:RAR:RXR

Stable Identifier

R-HSA-5634103

Type

Reaction [dissociation]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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SUMO-CRABP2 dissociates from atRA:RAR:RXR

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In the nucleus, cellular retinoic acid binding protein 2 (CRABP2), bound to all trans retinoic acid (atRA), directly binds to heterodimeric nuclear retinoic acid receptors (RAR:RXR) to form a complex through which atRA is channeled from the binding protein to RAR (Majumdar et al. 2011). The RAR:RXR heterodimer can be formed between any of three receptor isoforms for each; RARA, RARB, or RARG with RXRA, RXRB, or RXRG (Neiderreither and Dolle 2008). RARA requires sumoylation and phosphorylation for ligand binding and nuclear localisation (Zhu et al. 2009, Santos & Kim 2010).

RAR:RXR bind to their RA response elements (RARE, composed of tandem direct repeats of 5'-AGGTCA-3' spaced by either 2 bp or 5 bp (DR2, DR5) in response to their physiological ligand atRA, and regulate gene expression in various biological processes.

Literature References

PubMed ID	Title	Journal	Year
20215566	Activity of retinoic acid receptor-alpha is directly regulated at its protein kinase A sites in response to follicle-stimulating hormone signaling Santos, NC, Kim, KH	Endocrinology	2010
21998312	Nuclear translocation of cellular retinoic acid-binding protein II is regulated by retinoic acid-controlled SUMOylation Noy, N, Majumdar, A, Petrescu, AD, Xiong, Y	J. Biol. Chem.	2011
19850744	Small ubiquitin-like modifier-2 modification of retinoic acid receptor-alpha regulates its subcellular localization and transcriptional activity Santos, NC, Zhu, L, Kim, KH	Endocrinology	2009
18542081	Retinoic acid in development: towards an integrated view Niederreither, K, Dollé, P	Nat. Rev. Genet.	2008