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{
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"name": {
"name": "Rab GTPase family 4 (Rab4)",
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},
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{
"text": "<p>Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. [[cite:PUB00039681], [cite:PUB00091889], [cite:PUB00117387], [cite:PUB00117388], [cite:PUB00020223], [cite:PUB00087750], [cite:PUB00087751], [cite:PUB00113400], [cite:PUB00087752], [cite:PUB00087753], [cite:PUB00087754], [cite:PUB00087755], [cite:PUB00087756], [cite:PUB00087757], [cite:PUB00087758], [cite:PUB00087759], [cite:PUB00087760], [cite:PUB00087761], [cite:PUB00087632], [cite:PUB00087763], [cite:PUB00087764], [cite:PUB00087765]]</p>",
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"title": "Multiple aspects of Rab protein action in the secretory pathway: focus on Rab3 and Rab6.",
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"medline_journal": "Biochimie",
"ISO_journal": "Biochimie",
"authors": [
"Darchen F",
"Goud B."
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"authors": [
"Huber SK",
"Scheidig AJ."
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"issue": "16",
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"title": "Structural clues to Rab GTPase functional diversity.",
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"Pfeffer SR."
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"volume": "113 Pt 2",
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"year": 2000,
"title": "Rab GTPases coordinate endocytosis.",
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"medline_journal": "J Cell Sci",
"ISO_journal": "J. Cell. Sci.",
"authors": [
"Somsel Rodman J",
"Wandinger-Ness A."
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"issue": "100",
"year": 2001,
"title": "Ypt/rab gtpases: regulators of protein trafficking.",
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"Segev N."
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"title": "Vesicle transport: a close collaboration of Rabs and effectors.",
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"medline_journal": "Curr Biol",
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"authors": [
"Spang A."
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"title": "Rabs, Rips, FIPs, and endocytic membrane traffic.",
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"authors": [
"Prekeris R."
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"title": "How do Rab proteins function in membrane traffic?",
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"medline_journal": "Int J Biochem Cell Biol",
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"authors": [
"Armstrong J."
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"title": "Rab and ARF GTPase regulation of exocytosis.",
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"medline_journal": "Mol Membr Biol",
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"authors": [
"Collins RN."
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"year": 2002,
"title": "Direct interactions between rab GTPases and cargo.",
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"medline_journal": "Mol Cell",
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"authors": [
"Smythe E."
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"year": 2004,
"title": "Rab4 is an essential regulator of lysosomal trafficking in trypanosomes.",
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"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Hall BS",
"Pal A",
"Goulding D",
"Field MC."
],
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"title": "Rabs grab motors: defining the connections between Rab GTPases and motor proteins.",
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"authors": [
"Hammer JA 3rd",
"Wu XS."
],
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"title": "Rab proteins as membrane organizers.",
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"medline_journal": "Nat Rev Mol Cell Biol",
"ISO_journal": "Nat. Rev. Mol. Cell Biol.",
"authors": [
"Zerial M",
"McBride H."
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"title": "Ypt and Rab GTPases: insight into functions through novel interactions.",
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"medline_journal": "Curr Opin Cell Biol",
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"authors": [
"Segev N."
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"title": "Rab GTPases, intracellular traffic and disease.",
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"medline_journal": "Trends Mol Med",
"ISO_journal": "Trends Mol Med",
"authors": [
"Seabra MC",
"Mules EH",
"Hume AN."
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"DOI_URL": "https://doi.org/10.1016/S1471-4914(01)02227-4"
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"year": 2006,
"title": "Rab4GTPase modulates CFTR function by impairing channel expression at plasma membrane.",
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"raw_pages": "184-91",
"medline_journal": "Biochem Biophys Res Commun",
"ISO_journal": "Biochem Biophys Res Commun",
"authors": [
"Saxena SK",
"Kaur S",
"George C."
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"year": 2003,
"title": "Regulation of membrane transport by rab GTPases.",
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"medline_journal": "Crit Rev Biochem Mol Biol",
"ISO_journal": "Crit. Rev. Biochem. Mol. Biol.",
"authors": [
"Deneka M",
"Neeft M",
"van der Sluijs P."
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"title": "Rab4 GTP/GDP modulates amiloride-sensitive sodium channel (ENaC) function in colonic epithelia.",
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"medline_journal": "Biochem Biophys Res Commun",
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"authors": [
"Saxena SK",
"Singh M",
"Shibata H",
"Kaur S",
"George C."
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"title": "Rab GTPases: specifying and deciphering organelle identity and function.",
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"medline_journal": "Trends Cell Biol",
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"authors": [
"Pfeffer SR."
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"title": "Structural basis for Rab function: an overview.",
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"medline_journal": "Methods Enzymol",
"ISO_journal": "Meth. Enzymol.",
"authors": [
"Moyer BD",
"Balch WE."
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"title": "The Arabidopsis Rab GTPase family: another enigma variation.",
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"authors": [
"Rutherford S",
"Moore I."
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"authors": [
"Stenmark H",
"Olkkonen VM."
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}
