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Gene Review

RILP  -  Rab interacting lysosomal protein

Homo sapiens

Synonyms: FLJ31193, PP10141, Rab-interacting lysosomal protein
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Disease relevance of RILP


High impact information on RILP


Biological context of RILP

  • Recently, Rab7 and RILP have been found to be key proteins also for the biogenesis of phagolysosomes [5].
  • In addition, we have assigned the human PRA1 gene to chromosome 19q13.13-q13.2 and the human RILP gene to chromosome 17p13.3 [6].
  • In this study we assessed the functionality of the prenylation motif, protein kinase A (PKA) phosphorylation sites and nuclear localization sequences (NLSs) of RILP [7].
  • [(3)H]-mevalonolactone labeled endogenous RILP, showing that RILP is indeed prenylated, while phosphorylation analysis showed that the two PKA sites are phosphorylated [7].
  • We previously identified a nuclear envelope protein repressor element-1 silencing transcription factor (REST)/neuron-restrictive silencer factor (NRSF)-interacting Lin-11, Isl-1 and Mec-3 (LIM) domain protein (RILP) that we proposed functions in the nuclear translocation of the transcriptional repressor REST/NRSF [7].

Anatomical context of RILP


Physical interactions of RILP

  • This provides additional evidence that RILP interacts with REST/NRSF and REST4 in vivo, and is involved in the nuclear localization of REST/NRSF and REST4 [7].
  • We demonstrated that VPS22 interacts with the N-terminal half of RILP [9].
  • Both GST pull-down experiments and direct binding assays in vitro demonstrate that RILP interacts selectively with the wild-type and GTP-restricted but not GDP-restricted form of Rab34 [10].

Regulatory relationships of RILP

  • Expression of EGFP-tagged Rab34 wild-type or GTP-restricted forms in mammalian cells results in redistribution of clustered lysosomes to the peri-Golgi region and this property depends on K82, suggesting that Rab34 regulates lysosome distribution via interaction with RILP [10].

Other interactions of RILP

  • A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34 [8].
  • The 0.8-kb mRNA for human PRA1 is ubiquitously expressed, while the two mRNAs for RILP are differentially expressed [6].
  • These results show that RILP is required for REST/NRSF nuclear targeting and function [7].
  • The N-terminal and C-terminal half of RILP mediate interaction with VPS22 and VPS36, respectively [11].
  • We show here that the early machinery is integrated with the late machinery through a novel regulatory loop in which RILP interacts with VPS22 and VPS36 of ESCRT-II to mediate their membrane recruitment [11].

Analytical, diagnostic and therapeutic context of RILP


  1. Salmonella impairs RILP recruitment to Rab7 during maturation of invasion vacuoles. Harrison, R.E., Brumell, J.H., Khandani, A., Bucci, C., Scott, C.C., Jiang, X., Finlay, B.B., Grinstein, S. Mol. Biol. Cell (2004) [Pubmed]
  2. Structural basis for recruitment of RILP by small GTPase Rab7. Wu, M., Wang, T., Loh, E., Hong, W., Song, H. EMBO J. (2005) [Pubmed]
  3. Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. Cantalupo, G., Alifano, P., Roberti, V., Bruni, C.B., Bucci, C. EMBO J. (2001) [Pubmed]
  4. Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP. Harrison, R.E., Bucci, C., Vieira, O.V., Schroer, T.A., Grinstein, S. Mol. Cell. Biol. (2003) [Pubmed]
  5. The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is capable of self-interaction. Colucci, A.M., Campana, M.C., Bellopede, M., Bucci, C. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  6. Expression analysis and chromosomal assignment of PRA1 and RILP genes. Bucci, C., De Gregorio, L., Bruni, C.B. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  7. Characterization of the REST/NRSF-interacting LIM domain protein (RILP): localization and interaction with REST/NRSF. Shimojo, M., Hersh, L.B. J. Neurochem. (2006) [Pubmed]
  8. A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34. Wang, T., Wong, K.K., Hong, W. Mol. Biol. Cell (2004) [Pubmed]
  9. RILP interacts with the VPS22 component of the ESCRT-II complex. Progida, C., Spinosa, M.R., De Luca, A., Bucci, C. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  10. Assay and functional properties of Rab34 interaction with RILP in lysosome morphogenesis. Wang, T., Hong, W. Meth. Enzymol. (2005) [Pubmed]
  11. RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment. Wang, T., Hong, W. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
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