RNA-binding?

^a Direct interaction between FMRP and specific proteins has been documented using the power of the yeast two-hybrid selection method; other approaches such as co-immunoprecipitation allow detection of proteins that are associated with the ribonucleoprotein complexes but not a priori in direct contact with FMRP. Immunoprecipitation is a powerful tool to study proteins that are complexed to the targeted protein, and associated proteins are interpreted as reflecting the in vivo interactions. However, it has been shown that RNA-binding proteins might possibly re-associate with other components after cell lysis as a result of interaction of molecules in the cell extract, and so interactions identified by immunoprecipitation might not reflect the bone fide in vivo state of complexes (Ref. 105).
Abbreviations: CYFIP1/CYFIP2, cytoplasmic FMRP-interacting protein 1/2; 82-FIP, 82 kDa FMRP-interacting protein; FXR1P/FXR2P, proteins encoded by fragile-X-related genes 1 and 2; MSP58, microspherule protein 58; NUFIP1, nuclear FMRP-interacting protein 1.

16 Zhang, Y. et al. (1995) The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2. Embo J 14, 5358-5366, PubMed

48 Bardoni, B. et al. (2003) 82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization. Hum Mol Genet 12, 1689-1698, PubMed

49 Davidovic, L. et al. (2006) The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons. Hum Mol Genet, PubMed [Epub ahead of print]

50 Ohashi, S. et al. (2002) Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor. J Biol Chem 277, 37804-37810, PubMed

51 Menon, R.P., Gibson, T.J. and Pastore, A. (2004) The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre. J Mol Biol 343, 43-53, PubMed

53 Schenck, A. et al. (2001) A highly conserved protein family interacting with the fragile X mental retardation protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P. Proc Natl Acad Sci U S A 98, 8844-8849, PubMed

101 Siomi, M.C. et al. (1995) FXR1, an autosomal homolog of the fragile X mental retardation gene. Embo J 14, 2401-2408, PubMed

102 Bardoni, B., Schenck, A. and Mandel, J.L. (1999) A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein. Hum Mol Genet 8, 2557-2566, PubMed

103 Ceman, S., Brown, V. and Warren, S.T. (1999) Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X-related proteins as components of the complex. Mol Cell Biol 19, 7925-7932, PubMed

104 Ceman, S., Nelson, R. and Warren, S.T. (2000) Identification of mouse YB1/p50 as a component of the FMRP-associated mRNP particle. Biochem Biophys Res Commun 279, 904-908, PubMed

105 Mili, S. and Steitz, J.A. (2004) Evidence for reassociation of RNA-binding proteins after cell lysis: implications for the interpretation of immunoprecipitation analyses. Rna 10, 1692-1694, PubMed