RILP (gene)

RILP (gene)

Rab interacting lysosomal protein, also known as RILP, is a human gene.cite web | title = Entrez Gene: RILP Rab interacting lysosomal protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83547| accessdate = ]

PBB_Summary
section_title =
summary_text = RILP, along with the GTPase RAB7 (MIM 602298), controls late endocytic transport. [supplied by OMIM] cite web | title = Entrez Gene: RILP Rab interacting lysosomal protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83547| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Cantalupo G, Alifano P, Roberti V, "et al." |title=Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. |journal=EMBO J. |volume=20 |issue= 4 |pages= 683–93 |year= 2001 |pmid= 11179213 |doi= 10.1093/emboj/20.4.683
*cite journal | author=Bucci C, De Gregorio L, Bruni CB |title=Expression analysis and chromosomal assignment of PRA1 and RILP genes. |journal=Biochem. Biophys. Res. Commun. |volume=286 |issue= 4 |pages= 815–9 |year= 2001 |pmid= 11520070 |doi= 10.1006/bbrc.2001.5466
*cite journal | author=Jordens I, Fernandez-Borja M, Marsman M, "et al." |title=The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors. |journal=Curr. Biol. |volume=11 |issue= 21 |pages= 1680–5 |year= 2002 |pmid= 11696325 |doi=
*cite journal | author=Wang T, Hong W |title=Interorganellar regulation of lysosome positioning by the Golgi apparatus through Rab34 interaction with Rab-interacting lysosomal protein. |journal=Mol. Biol. Cell |volume=13 |issue= 12 |pages= 4317–32 |year= 2003 |pmid= 12475955 |doi= 10.1091/mbc.E02-05-0280
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Cardoso C, Leventer RJ, Ward HL, "et al." |title=Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3. |journal=Am. J. Hum. Genet. |volume=72 |issue= 4 |pages= 918–30 |year= 2003 |pmid= 12621583 |doi=
*cite journal | author=Harrison RE, Bucci C, Vieira OV, "et al." |title=Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP. |journal=Mol. Cell. Biol. |volume=23 |issue= 18 |pages= 6494–506 |year= 2003 |pmid= 12944476 |doi=
*cite journal | author=Wang T, Wong KK, Hong W |title=A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34. |journal=Mol. Biol. Cell |volume=15 |issue= 2 |pages= 815–26 |year= 2004 |pmid= 14668488 |doi= 10.1091/mbc.E03-06-0413
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Wan D, Gong Y, Qin W, "et al." |title=Large-scale cDNA transfection screening for genes related to cancer development and progression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 44 |pages= 15724–9 |year= 2004 |pmid= 15498874 |doi= 10.1073/pnas.0404089101
*cite journal | author=Wu M, Wang T, Loh E, "et al." |title=Structural basis for recruitment of RILP by small GTPase Rab7. |journal=EMBO J. |volume=24 |issue= 8 |pages= 1491–501 |year= 2005 |pmid= 15933719 |doi= 10.1038/sj.emboj.7600643
*cite journal | author=Colucci AM, Campana MC, Bellopede M, Bucci C |title=The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is capable of self-interaction. |journal=Biochem. Biophys. Res. Commun. |volume=334 |issue= 1 |pages= 128–33 |year= 2005 |pmid= 15996637 |doi= 10.1016/j.bbrc.2005.06.067
*cite journal | author=Shimojo M, Hersh LB |title=Characterization of the REST/NRSF-interacting LIM domain protein (RILP): localization and interaction with REST/NRSF. |journal=J. Neurochem. |volume=96 |issue= 4 |pages= 1130–8 |year= 2006 |pmid= 16417580 |doi= 10.1111/j.1471-4159.2005.03608.x
*cite journal | author=Marsman M, Jordens I, Rocha N, "et al." |title=A splice variant of RILP induces lysosomal clustering independent of dynein recruitment. |journal=Biochem. Biophys. Res. Commun. |volume=344 |issue= 3 |pages= 747–56 |year= 2006 |pmid= 16631113 |doi= 10.1016/j.bbrc.2006.03.178
*cite journal | author=Progida C, Spinosa MR, De Luca A, Bucci C |title=RILP interacts with the VPS22 component of the ESCRT-II complex. |journal=Biochem. Biophys. Res. Commun. |volume=347 |issue= 4 |pages= 1074–9 |year= 2006 |pmid= 16857164 |doi= 10.1016/j.bbrc.2006.07.007

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать курсовую

Look at other dictionaries:

  • RABAC1 — Rab acceptor 1 (prenylated), also known as RABAC1, is a human gene.cite web | title = Entrez Gene: RABAC1 Rab acceptor 1 (prenylated)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=10567| accessdate = ]… …   Wikipedia

  • RAB34 — RAB34, member RAS oncogene family, also known as RAB34, is a human gene.cite web | title = Entrez Gene: RAB34 RAB34, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=83871|… …   Wikipedia

  • Dynactin — or Dynein activator complex is a multi subunit protein found in eukaryotic cells that aids in bidirectional intracellular transport by binding to dynein and Kinesin II and linking them to the organelle or vesicle to be transported.[1][2] Contents …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”