RAB11FIP5: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Rab11 family-interacting protein 5''' is a [[protein]] that in humans is encoded by the ''RAB11FIP5'' [[gene]].<ref name="pmid10048485">{{cite journal | vauthors = Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Research | volume = 5 | issue = 6 | pages = 355–64 | date = December 1998 | pmid = 10048485 | pmc =  | doi = 10.1093/dnares/5.6.355 }}</ref><ref name="pmid11163216">{{cite journal | vauthors = Prekeris R, Klumperman J, Scheller RH | title = A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes | journal = Molecular Cell | volume = 6 | issue = 6 | pages = 1437–48 | date = December 2000 | pmid = 11163216 | pmc =  | doi = 10.1016/S1097-2765(00)00140-4 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RAB11FIP5 RAB11 family interacting protein 5 (class I)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26056| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = RAB11 family interacting protein 5 (class I)
| HGNCid = 24845
| Symbol = RAB11FIP5
| AltSymbols =; DKFZP434H018; GAF1; KIAA0857; RIP11; pp75
| OMIM = 605536
| ECnumber = 
| Homologene = 9158
| MGIid = 1098586
| GeneAtlas_image1 = PBB_GE_RAB11FIP5_210879_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043015 |text = gamma-tubulin binding}}
| Component = {{GNF_GO|id=GO:0005741 |text = mitochondrial outer membrane}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 26056
    | Hs_Ensembl = ENSG00000135631
    | Hs_RefseqProtein = NP_056285
    | Hs_RefseqmRNA = NM_015470
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 73154019
    | Hs_GenLoc_end = 73193654
    | Hs_Uniprot = Q9BXF6
    | Mm_EntrezGene = 52055
    | Mm_Ensembl = ENSMUSG00000051343
    | Mm_RefseqmRNA = XM_992559
    | Mm_RefseqProtein = XP_997653
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 85300620
    | Mm_GenLoc_end = 85340292
    | Mm_Uniprot = Q3UM85
  }}
}}
'''RAB11 family interacting protein 5 (class I)''', also known as '''RAB11FIP5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAB11FIP5 RAB11 family interacting protein 5 (class I)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26056| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
RAB11FIP5 has been shown to [[Protein-protein interaction|interact]] with [[RAB11A]]<ref name=pmid11163216 /><ref name=pmid11495908>{{cite journal | vauthors = Hales CM, Griner R, Hobdy-Henderson KC, Dorn MC, Hardy D, Kumar R, Navarre J, Chan EK, Lapierre LA, Goldenring JR | title = Identification and characterization of a family of Rab11-interacting proteins | journal = The Journal of Biological Chemistry | volume = 276 | issue = 42 | pages = 39067–75 | date = October 2001 | pmid = 11495908 | doi = 10.1074/jbc.M104831200 }}</ref><ref name=pmid11481332>{{cite journal | vauthors = Prekeris R, Davies JM, Scheller RH | title = Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins | journal = The Journal of Biological Chemistry | volume = 276 | issue = 42 | pages = 38966–70 | date = October 2001 | pmid = 11481332 | doi = 10.1074/jbc.M106133200 }}</ref> and [[RAB25]].<ref name=pmid11495908/><ref name=pmid11481332/>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
==Vesicle trafficking==  
{{reflist|2}}
==Further reading==
Rab11FIP5 is one of the many proteins that have been shown to interact with the Rab11 protein.<ref name=pmid11495908/> Rab GTPases, such as Rab11, are enzymes that are involved in vesicular trafficking. Rab11 specifically plays a key role in endocytic trafficking and recycling through guiding early endosomes to endosome recycling complexes.<ref name="Grant_2009">{{cite journal | vauthors = Grant BD, Donaldson JG | title = Pathways and mechanisms of endocytic recycling | journal = Nature Reviews. Molecular Cell Biology | volume = 10 | issue = 9 | pages = 597–608 | year = 2009 | pmid = 19696797 | pmc = 3038567 | doi = 10.1038/nrm2755 }}</ref> Rab11FIP5, like most other Rab11FIP proteins, interacts with Rab11 by serving as an adaptor protein. This leads to downstream changes with regards to which proteins can interact. This is a result of the various Rab11FIP proteins that each have different binding partners. This process allows for the coordination and organization of endosomal transport and ultimately gives Rab11 its versatile function in the cell.<ref name="Grant_2009" /> It is believed that Rab11 recruits specific Rab11FIP proteins to the surface of vesicles in order to determine how the vesicle will behave.<ref name= "Schonteich_2008">{{cite journal | vauthors = Schonteich E, Wilson GM, Burden J, Hopkins CR, Anderson K, Goldenring JR, Prekeris R | title = The Rip11/Rab11-FIP5 and kinesin II complex regulates endocytic protein recycling | journal = Journal of Cell Science | volume = 121 | issue = Pt 22 | pages = 3824-33 | date = November 2008 | pmid = 18957512 | doi = 10.1242/jcs.032441 }}</ref>
{{refbegin | 2}}
   
{{PBB_Further_reading
Studies have shown that Rab11FIP5 localizes to the perinuclear endosomes where it aids in sorting vesicles into the slow recycling route.<ref name= "Schonteich_2008"/> This process involves the transport of cargo proteins, like endocytosed receptors, to endosome recycling complexes and subsequently to the plasma membrane. This is in contrast to the fast constitutive recycling route which allows for the direct transport of cargo from the endosome to the plasma membrane.<ref name="Schonteich_2008"/> Rab11FIP5 aids in this sorting process by binding to kinesin II and forming a protein complex to regulate vesicular trafficking. Some of the proteins that are regulated through Rab11FIP5 mediated vesicle trafficking are microtubule proteins and the TfR receptor. This links Rab11FIP5 functionality to the cell cytoskeleton and the iron uptake of a cell, respectively.<ref name="Schonteich_2008"/>
| citations =
   
*{{cite journal  | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 6 |pages= 355-64 |year= 1999 |pmid= 10048485 |doi=  }}
==Other functions==
*{{cite journal  | author=Wang D, Buyon JP, Zhu W, Chan EK |title=Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and identification of distinct human autoantibodies. |journal=J. Clin. Invest. |volume=104 |issue= 9 |pages= 1265-75 |year= 1999 |pmid= 10545525 |doi= }}
   
*{{cite journal | author=Prekeris R, Klumperman J, Scheller RH |title=A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes. |journal=Mol. Cell |volume=6 |issue= 6 |pages= 1437-48 |year= 2001 |pmid= 11163216 |doi= }}
Rab11FIP5 has been shown to play a role in the nervous system because it functions in neurons. Studies have suggested that Rab11FIP5 is involved in regulating the localization of the postsynaptic AMPA-type glutamate receptor. The AMPA receptor is an excitatory receptor that can be found on the plasma membranes of neurons. Studies have shown that mice with the Rab11FIP5 gene knocked out have severe long term neuronal depression. Without the presence of Rab11FIP5, it is hypothesized that the internalized AMPA receptors cannot be recycled back onto the plasma membrane because the receptors cannot be correctly trafficked to intracellular organelles responsible for recycling.<ref name= "Bacaj_2015">{{cite journal | vauthors = Bacaj T, Ahmad M, Jurado S, Malenka RC, Südhof TC | title = Synaptic Function of Rab11Fip5: Selective Requirement for Hippocampal Long-Term Depression | journal = The Journal of Neuroscience | volume = 35 | issue = 19 | pages = 7460–74 | date = May 2015 | pmid = 25972173 | doi = 10.1523/JNEUROSCI.1581-14.2015 }}</ref>
*{{cite journal  | author=Chen D, Xu W, He P, ''et al.'' |title=Gaf-1, a gamma -SNAP-binding protein associated with the mitochondria. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13127-35 |year= 2001 |pmid= 11278501 |doi= 10.1074/jbc.M009424200 }}
   
*{{cite journal  | author=Prekeris R, Davies JM, Scheller RH |title=Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 38966-70 |year= 2001 |pmid= 11481332 |doi= 10.1074/jbc.M106133200 }}
Rab11FIP5 has also been implicated as a protein involved in the creation of tissue polarity during development. Rab11FIP5 has been shown to be involved in the vesicle trafficking and degradation of proteins used to coordinate embryonic development. This is conducted in a manner that helps maintain the ectoderm polarity in embryonic Drosophila.<ref name="Calero-Cuenca_2016">{{cite journal | vauthors = Calero-Cuenca FJ, Sotillos S | title = Nuf and Rip11 requirement for polarity determinant recycling during Drosophila development | journal = Small GTPases | pages = 1-8 | date = September 2016 | pmid = 27687567 | doi = 10.1080/21541248.2016.1235386 }}</ref>
*{{cite journal | author=Hales CM, Griner R, Hobdy-Henderson KC, ''et al.'' |title=Identification and characterization of a family of Rab11-interacting proteins. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39067-75 |year= 2001 |pmid= 11495908 |doi= 10.1074/jbc.M104831200 }}
   
*{{cite journal | author=Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW |title=Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells. |journal=Biochem. Biophys. Res. Commun. |volume=299 |issue= 5 |pages= 770-9 |year= 2003 |pmid= 12470645 |doi=  }}
Rab11FIP5 is also suggested to be involved in aiding salivary epithelial cells to adjust to extracellular pH. V-ATPase, a proton pump protein, has been shown to be reliant on Rab11FIP5 mediated vesicle trafficking. When Rab11FIP5 is knocked down, salivary cells cannot correctly translocate V-ATPase to the plasma membrane in response to extracellular acidosis. While this pathway remains largely unknown, these results suggest a link between Rab11FIP5 function and the maintenance of the buffering capacity of saliva.<ref name="Oehlke_2010">{{cite journal | vauthors = Oehlke O, Martin HW, Osterberg N, Roussa E | title = Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts | journal = Journal of Cellular Physiology | volume = 226 | issue = 3 | pages = 638–51 | date = March 2011 | pmid = 20717956 | doi = 10.1002/jcp.22388 }}</ref>
*{{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=Tani K, Shibata M, Kawase K, ''et al.'' |title=Mapping of functional domains of gamma-SNAP. |journal=J. Biol. Chem. |volume=278 |issue= 15 |pages= 13531-8 |year= 2003 |pmid= 12554740 |doi= 10.1074/jbc.M213205200 }}
*{{cite journal | author=Kawase K, Shibata M, Kawashima H, ''et al.'' |title=Gaf-1b is an alternative splice variant of Gaf-1/Rip11. |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 4 |pages= 1042-6 |year= 2003 |pmid= 12684040 |doi=  }}
*{{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=Brill LM, Salomon AR, Ficarro SB, ''et al.'' |title=Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. |journal=Anal. Chem. |volume=76 |issue= 10 |pages= 2763-72 |year= 2004 |pmid= 15144186 |doi= 10.1021/ac035352d }}
*{{cite journal | author=Jin J, Smith FD, Stark C, ''et al.'' |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436-50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 }}
*{{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=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{cite journal | author=Schwenk RW, Luiken JJ, Eckel J |title=FIP2 and Rip11 specify Rab11a-mediated cellular distribution of GLUT4 and FAT/CD36 in H9c2-hIR cells. |journal=Biochem. Biophys. Res. Commun. |volume=363 |issue= 1 |pages= 119-25 |year= 2007 |pmid= 17854769 |doi= 10.1016/j.bbrc.2007.08.111 }}
}}
{{refend}}


{{protein-stub}}
== References ==
{{WikiDoc Sources}}
{{Reflist|33em}}
 
== Further reading ==
{{Refbegin|33em}}
* {{cite journal | vauthors = Wang D, Buyon JP, Zhu W, Chan EK | title = Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and identification of distinct human autoantibodies | journal = The Journal of Clinical Investigation | volume = 104 | issue = 9 | pages = 1265–75 | date = November 1999 | pmid = 10545525 | pmc = 409828 | doi = 10.1172/JCI8003 }}
* {{cite journal | vauthors = Chen D, Xu W, He P, Medrano EE, Whiteheart SW | title = Gaf-1, a gamma -SNAP-binding protein associated with the mitochondria | journal = The Journal of Biological Chemistry | volume = 276 | issue = 16 | pages = 13127–35 | date = April 2001 | pmid = 11278501 | doi = 10.1074/jbc.M009424200 }}
* {{cite journal | vauthors = Prekeris R, Davies JM, Scheller RH | title = Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins | journal = The Journal of Biological Chemistry | volume = 276 | issue = 42 | pages = 38966–70 | date = October 2001 | pmid = 11481332 | doi = 10.1074/jbc.M106133200 }}
* {{cite journal | vauthors = Hales CM, Griner R, Hobdy-Henderson KC, Dorn MC, Hardy D, Kumar R, Navarre J, Chan EK, Lapierre LA, Goldenring JR | title = Identification and characterization of a family of Rab11-interacting proteins | journal = The Journal of Biological Chemistry | volume = 276 | issue = 42 | pages = 39067–75 | date = October 2001 | pmid = 11495908 | doi = 10.1074/jbc.M104831200 }}
* {{cite journal | vauthors = Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW | title = Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells | journal = Biochemical and Biophysical Research Communications | volume = 299 | issue = 5 | pages = 770–9 | date = December 2002 | pmid = 12470645 | doi = 10.1016/S0006-291X(02)02720-1 }}
* {{cite journal | vauthors = Tani K, Shibata M, Kawase K, Kawashima H, Hatsuzawa K, Nagahama M, Tagaya M | title = Mapping of functional domains of gamma-SNAP | journal = The Journal of Biological Chemistry | volume = 278 | issue = 15 | pages = 13531–8 | date = April 2003 | pmid = 12554740 | doi = 10.1074/jbc.M213205200 }}
* {{cite journal | vauthors = Kawase K, Shibata M, Kawashima H, Hatsuzawa K, Nagahama M, Tagaya M, Tani K | title = Gaf-1b is an alternative splice variant of Gaf-1/Rip11 | journal = Biochemical and Biophysical Research Communications | volume = 303 | issue = 4 | pages = 1042–6 | date = April 2003 | pmid = 12684040 | doi = 10.1016/S0006-291X(03)00486-8 }}
* {{cite journal | vauthors = Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC | title = Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry | journal = Analytical Chemistry | volume = 76 | issue = 10 | pages = 2763–72 | date = May 2004 | pmid = 15144186 | doi = 10.1021/ac035352d }}
* {{cite journal | vauthors = Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization | journal = Current Biology | volume = 14 | issue = 16 | pages = 1436–50 | date = August 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 }}
* {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = November 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 }}
* {{cite journal | vauthors = Schwenk RW, Luiken JJ, Eckel J | title = FIP2 and Rip11 specify Rab11a-mediated cellular distribution of GLUT4 and FAT/CD36 in H9c2-hIR cells | journal = Biochemical and Biophysical Research Communications | volume = 363 | issue = 1 | pages = 119–25 | date = November 2007 | pmid = 17854769 | doi = 10.1016/j.bbrc.2007.08.111 }}
{{Refend}}

Revision as of 02:25, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Rab11 family-interacting protein 5 is a protein that in humans is encoded by the RAB11FIP5 gene.[1][2][3]

Interactions

RAB11FIP5 has been shown to interact with RAB11A[2][4][5] and RAB25.[4][5]

Vesicle trafficking

Rab11FIP5 is one of the many proteins that have been shown to interact with the Rab11 protein.[4] Rab GTPases, such as Rab11, are enzymes that are involved in vesicular trafficking. Rab11 specifically plays a key role in endocytic trafficking and recycling through guiding early endosomes to endosome recycling complexes.[6] Rab11FIP5, like most other Rab11FIP proteins, interacts with Rab11 by serving as an adaptor protein. This leads to downstream changes with regards to which proteins can interact. This is a result of the various Rab11FIP proteins that each have different binding partners. This process allows for the coordination and organization of endosomal transport and ultimately gives Rab11 its versatile function in the cell.[6] It is believed that Rab11 recruits specific Rab11FIP proteins to the surface of vesicles in order to determine how the vesicle will behave.[7]

Studies have shown that Rab11FIP5 localizes to the perinuclear endosomes where it aids in sorting vesicles into the slow recycling route.[7] This process involves the transport of cargo proteins, like endocytosed receptors, to endosome recycling complexes and subsequently to the plasma membrane. This is in contrast to the fast constitutive recycling route which allows for the direct transport of cargo from the endosome to the plasma membrane.[7] Rab11FIP5 aids in this sorting process by binding to kinesin II and forming a protein complex to regulate vesicular trafficking. Some of the proteins that are regulated through Rab11FIP5 mediated vesicle trafficking are microtubule proteins and the TfR receptor. This links Rab11FIP5 functionality to the cell cytoskeleton and the iron uptake of a cell, respectively.[7]

Other functions

Rab11FIP5 has been shown to play a role in the nervous system because it functions in neurons. Studies have suggested that Rab11FIP5 is involved in regulating the localization of the postsynaptic AMPA-type glutamate receptor. The AMPA receptor is an excitatory receptor that can be found on the plasma membranes of neurons. Studies have shown that mice with the Rab11FIP5 gene knocked out have severe long term neuronal depression. Without the presence of Rab11FIP5, it is hypothesized that the internalized AMPA receptors cannot be recycled back onto the plasma membrane because the receptors cannot be correctly trafficked to intracellular organelles responsible for recycling.[8]

Rab11FIP5 has also been implicated as a protein involved in the creation of tissue polarity during development. Rab11FIP5 has been shown to be involved in the vesicle trafficking and degradation of proteins used to coordinate embryonic development. This is conducted in a manner that helps maintain the ectoderm polarity in embryonic Drosophila.[9]

Rab11FIP5 is also suggested to be involved in aiding salivary epithelial cells to adjust to extracellular pH. V-ATPase, a proton pump protein, has been shown to be reliant on Rab11FIP5 mediated vesicle trafficking. When Rab11FIP5 is knocked down, salivary cells cannot correctly translocate V-ATPase to the plasma membrane in response to extracellular acidosis. While this pathway remains largely unknown, these results suggest a link between Rab11FIP5 function and the maintenance of the buffering capacity of saliva.[10]

References

  1. ↑ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (December 1998). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
  2. ↑ 2.0 2.1 Prekeris R, Klumperman J, Scheller RH (December 2000). "A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes". Molecular Cell. 6 (6): 1437–48. doi:10.1016/S1097-2765(00)00140-4. PMID 11163216.
  3. ↑ "Entrez Gene: RAB11FIP5 RAB11 family interacting protein 5 (class I)".
  4. ↑ 4.0 4.1 4.2 Hales CM, Griner R, Hobdy-Henderson KC, Dorn MC, Hardy D, Kumar R, Navarre J, Chan EK, Lapierre LA, Goldenring JR (October 2001). "Identification and characterization of a family of Rab11-interacting proteins". The Journal of Biological Chemistry. 276 (42): 39067–75. doi:10.1074/jbc.M104831200. PMID 11495908.
  5. ↑ 5.0 5.1 Prekeris R, Davies JM, Scheller RH (October 2001). "Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins". The Journal of Biological Chemistry. 276 (42): 38966–70. doi:10.1074/jbc.M106133200. PMID 11481332.
  6. ↑ 6.0 6.1 Grant BD, Donaldson JG (2009). "Pathways and mechanisms of endocytic recycling". Nature Reviews. Molecular Cell Biology. 10 (9): 597–608. doi:10.1038/nrm2755. PMC 3038567. PMID 19696797.
  7. ↑ 7.0 7.1 7.2 7.3 Schonteich E, Wilson GM, Burden J, Hopkins CR, Anderson K, Goldenring JR, Prekeris R (November 2008). "The Rip11/Rab11-FIP5 and kinesin II complex regulates endocytic protein recycling". Journal of Cell Science. 121 (Pt 22): 3824–33. doi:10.1242/jcs.032441. PMID 18957512.
  8. ↑ Bacaj T, Ahmad M, Jurado S, Malenka RC, Südhof TC (May 2015). "Synaptic Function of Rab11Fip5: Selective Requirement for Hippocampal Long-Term Depression". The Journal of Neuroscience. 35 (19): 7460–74. doi:10.1523/JNEUROSCI.1581-14.2015. PMID 25972173.
  9. ↑ Calero-Cuenca FJ, Sotillos S (September 2016). "Nuf and Rip11 requirement for polarity determinant recycling during Drosophila development". Small GTPases: 1–8. doi:10.1080/21541248.2016.1235386. PMID 27687567.
  10. ↑ Oehlke O, Martin HW, Osterberg N, Roussa E (March 2011). "Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts". Journal of Cellular Physiology. 226 (3): 638–51. doi:10.1002/jcp.22388. PMID 20717956.

Further reading

  • Wang D, Buyon JP, Zhu W, Chan EK (November 1999). "Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and identification of distinct human autoantibodies". The Journal of Clinical Investigation. 104 (9): 1265–75. doi:10.1172/JCI8003. PMC 409828. PMID 10545525.
  • Chen D, Xu W, He P, Medrano EE, Whiteheart SW (April 2001). "Gaf-1, a gamma -SNAP-binding protein associated with the mitochondria". The Journal of Biological Chemistry. 276 (16): 13127–35. doi:10.1074/jbc.M009424200. PMID 11278501.
  • Prekeris R, Davies JM, Scheller RH (October 2001). "Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins". The Journal of Biological Chemistry. 276 (42): 38966–70. doi:10.1074/jbc.M106133200. PMID 11481332.
  • Hales CM, Griner R, Hobdy-Henderson KC, Dorn MC, Hardy D, Kumar R, Navarre J, Chan EK, Lapierre LA, Goldenring JR (October 2001). "Identification and characterization of a family of Rab11-interacting proteins". The Journal of Biological Chemistry. 276 (42): 39067–75. doi:10.1074/jbc.M104831200. PMID 11495908.
  • Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW (December 2002). "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells". Biochemical and Biophysical Research Communications. 299 (5): 770–9. doi:10.1016/S0006-291X(02)02720-1. PMID 12470645.
  • Tani K, Shibata M, Kawase K, Kawashima H, Hatsuzawa K, Nagahama M, Tagaya M (April 2003). "Mapping of functional domains of gamma-SNAP". The Journal of Biological Chemistry. 278 (15): 13531–8. doi:10.1074/jbc.M213205200. PMID 12554740.
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