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| | <StructureSection load='4d0g' size='340' side='right'caption='[[4d0g]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='4d0g' size='340' side='right'caption='[[4d0g]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d0g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D0G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d0g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D0G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0g OCA], [http://pdbe.org/4d0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d0g RCSB], [http://www.ebi.ac.uk/pdbsum/4d0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0g ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4d0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0g OCA], [https://pdbe.org/4d0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d0g RCSB], [https://www.ebi.ac.uk/pdbsum/4d0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RAB14_HUMAN RAB14_HUMAN]] Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion.<ref>PMID:22595670</ref> [[http://www.uniprot.org/uniprot/RFIP1_HUMAN RFIP1_HUMAN]] A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis.<ref>PMID:11786538</ref> <ref>PMID:15181150</ref> <ref>PMID:15355514</ref> <ref>PMID:16920206</ref> | + | [[https://www.uniprot.org/uniprot/RAB14_HUMAN RAB14_HUMAN]] Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion.<ref>PMID:22595670</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ras-related protein Rab|Ras-related protein Rab]] | + | *[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Khan, A R]] | + | [[Category: Khan AR]] |
| - | [[Category: Lall, P]] | + | [[Category: Lall P]] |
| - | [[Category: Effector recruitment]]
| + | |
| - | [[Category: Endosomal trafficking]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rab14 gtpase]]
| + | |
| Structural highlights
Function
[RAB14_HUMAN] Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion.[1]
Publication Abstract from PubMed
Rab GTPases recruit effector proteins, via their GTP-dependent switch regions, to distinct sub-cellular compartments. Rab11 and Rab25 are closely related small GTPases that bind to common effectors termed the Rab11-Family of Interacting Proteins (FIPs). The FIPs are organized into two subclasses (class I and class II) based on sequence and domain organization, and both subclasses contain a highly conserved Rab-binding domain (RBD) at their C-termini. Yeast two-hybrid and biochemical studies have revealed that the more distantly related Rab14 also interacts with class I FIPs. Here, we perform detailed structural, thermodynamic and cellular analyses of the interactions between Rab14 and one of the class I FIPs - the Rab Coupling Protein (RCP) - to clarify the molecular aspects of the interaction. We find that Rab14 indeed binds to RCP, albeit with reduced affinity relative to conventional Rab11:FIP and Rab25:FIP complexes. However, in vivo, Rab11 recruits RCP onto biological membranes. Furthermore, biophysical analyses reveal a non-canonical 1:2 stoichiometry between Rab14:RCP in dilute solutions, in contrast to Rab11/25 complexes. The structure of Rab14:RCP reveals that Rab14 interacts with the canonical RBD, and also provides insight into the unusual properties of the complex. Finally, we show that both the Rab Coupling Protein and Rab14 function in neuritogenesis.
Structure-Function Analyses of the Interactions Between Rab11 and Rab14 Small GTPases with their Shared Effector Rab Coupling Protein (RCP).,Lall P, Lindsay A, Hanscom S, Kecman T, Taglauer ES, McVeigh UM, Franklin E, McCaffrey MW, Khan AR J Biol Chem. 2015 May 31. pii: jbc.M114.612366. PMID:26032412[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Linford A, Yoshimura S, Nunes Bastos R, Langemeyer L, Gerondopoulos A, Rigden DJ, Barr FA. Rab14 and its exchange factor FAM116 link endocytic recycling and adherens junction stability in migrating cells. Dev Cell. 2012 May 15;22(5):952-66. doi: 10.1016/j.devcel.2012.04.010. PMID:22595670 doi:http://dx.doi.org/10.1016/j.devcel.2012.04.010
- ↑ Lall P, Lindsay A, Hanscom S, Kecman T, Taglauer ES, McVeigh UM, Franklin E, McCaffrey MW, Khan AR. Structure-Function Analyses of the Interactions Between Rab11 and Rab14 Small GTPases with their Shared Effector Rab Coupling Protein (RCP). J Biol Chem. 2015 May 31. pii: jbc.M114.612366. PMID:26032412 doi:http://dx.doi.org/10.1074/jbc.M114.612366
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