메뉴 건너뛰기




Volumn 21, Issue 5, 2010, Pages 611-620

Small peptide recognition sequence for intracellular sorting

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CELL SURFACE RECEPTORS; CELLULAR EVENTS; COAT PROTEINS; CYTOPLASMIC DOMAINS; ENDOCYTIC PATHWAYS; INTRACELLULAR COMPARTMENTS; MEMBRANE RECEPTORS; MOLECULAR SORTING; PEPTIDE RECOGNITION; PEPTIDE SEQUENCES; PEPTIDE SIGNALS; RECEPTOR PROTEINS; SEQUENCE MOTIFS; SHORT SIGNAL; SUBCELLULAR COMPARTMENTS; TRANSMEMBRANE RECEPTORS;

EID: 77957366859     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2010.08.007     Document Type: Review
Times cited : (30)

References (93)
  • 1
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 2003, 72:395-447.
    • (2003) Annu Rev Biochem , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 2
    • 0037171443 scopus 로고    scopus 로고
    • Conserved mammalian gonadotropin-releasing hormone receptor carboxyl terminal amino acids regulate ligand binding, effector coupling and internalization
    • Brothers S.P., Janovick J.A., Maya-Nunez G., Cornea A., Han X.B., Conn P.M. Conserved mammalian gonadotropin-releasing hormone receptor carboxyl terminal amino acids regulate ligand binding, effector coupling and internalization. Mol Cell Endocrinol 2002, 190:19-27.
    • (2002) Mol Cell Endocrinol , vol.190 , pp. 19-27
    • Brothers, S.P.1    Janovick, J.A.2    Maya-Nunez, G.3    Cornea, A.4    Han, X.B.5    Conn, P.M.6
  • 3
    • 33747065914 scopus 로고    scopus 로고
    • Modulation of lipoprotein receptor functions by intracellular adaptor proteins
    • Stolt P.C., Bock H.H. Modulation of lipoprotein receptor functions by intracellular adaptor proteins. Cell Signal 2006, 18:1560-1571.
    • (2006) Cell Signal , vol.18 , pp. 1560-1571
    • Stolt, P.C.1    Bock, H.H.2
  • 4
    • 19444363531 scopus 로고    scopus 로고
    • Biology of natriuretic peptides and their receptors
    • Pandey K.N. Biology of natriuretic peptides and their receptors. Peptides 2005, 26:901-932.
    • (2005) Peptides , vol.26 , pp. 901-932
    • Pandey, K.N.1
  • 5
    • 12744281091 scopus 로고    scopus 로고
    • Constitutive and protein kinase C-induced internalization of the dopamine transporter is mediated by a clathrin-dependent mechanism
    • Sorkina T., Hoover B.R., Zahniser N.R., Sorkin A. Constitutive and protein kinase C-induced internalization of the dopamine transporter is mediated by a clathrin-dependent mechanism. Traffic 2005, 6:157-170.
    • (2005) Traffic , vol.6 , pp. 157-170
    • Sorkina, T.1    Hoover, B.R.2    Zahniser, N.R.3    Sorkin, A.4
  • 6
    • 0036220292 scopus 로고    scopus 로고
    • Single-handed recognition of a sorting traffic motif by the GGA proteins
    • Kirchhausen T. Single-handed recognition of a sorting traffic motif by the GGA proteins. Nat Struct Biol 2002, 9:241-244.
    • (2002) Nat Struct Biol , vol.9 , pp. 241-244
    • Kirchhausen, T.1
  • 7
    • 33747120931 scopus 로고    scopus 로고
    • Biosynthesis and trafficking of seven transmembrane receptor signalling complexes
    • Dupre D.J., Hebert T.E. Biosynthesis and trafficking of seven transmembrane receptor signalling complexes. Cell Signal 2006, 18:1549-1559.
    • (2006) Cell Signal , vol.18 , pp. 1549-1559
    • Dupre, D.J.1    Hebert, T.E.2
  • 8
    • 21844440569 scopus 로고    scopus 로고
    • Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis
    • Pelkmans L., Fava E., Grabner H., Hannus M., Habermann B., Krausz E., Zerial M. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature 2005, 436:78-86.
    • (2005) Nature , vol.436 , pp. 78-86
    • Pelkmans, L.1    Fava, E.2    Grabner, H.3    Hannus, M.4    Habermann, B.5    Krausz, E.6    Zerial, M.7
  • 9
    • 0037085298 scopus 로고    scopus 로고
    • Ligand-regulated internalization, trafficking, and down-regulation of guanylyl cyclase/atrial natriuretic peptide receptor-A in human embryonic kidney 293 cells
    • Pandey K.N., Nguyen H.T., Sharma G.D., Shi S.J., Kriegel A.M. Ligand-regulated internalization, trafficking, and down-regulation of guanylyl cyclase/atrial natriuretic peptide receptor-A in human embryonic kidney 293 cells. J Biol Chem 2002, 277:4618-4627.
    • (2002) J Biol Chem , vol.277 , pp. 4618-4627
    • Pandey, K.N.1    Nguyen, H.T.2    Sharma, G.D.3    Shi, S.J.4    Kriegel, A.M.5
  • 12
    • 37249092938 scopus 로고    scopus 로고
    • Endocytosis: a positive or a negative influence on Wnt signalling?
    • Gagliardi M., Piddini E., Vincent J.P. Endocytosis: a positive or a negative influence on Wnt signalling?. Traffic 2008, 9:1-9.
    • (2008) Traffic , vol.9 , pp. 1-9
    • Gagliardi, M.1    Piddini, E.2    Vincent, J.P.3
  • 13
    • 74949144637 scopus 로고    scopus 로고
    • Ligand-mediated endocytosis and intracellular sequestration of guanylyl cyclase/natriuretic peptide receptors: role of GDAY motif
    • Pandey K.N. Ligand-mediated endocytosis and intracellular sequestration of guanylyl cyclase/natriuretic peptide receptors: role of GDAY motif. Mol Cell Biochem 2010, 334:81-98.
    • (2010) Mol Cell Biochem , vol.334 , pp. 81-98
    • Pandey, K.N.1
  • 14
    • 0036341207 scopus 로고    scopus 로고
    • Signal transduction and endocytosis: close encounters of many kinds
    • Sorkin A., Von Zastrow M. Signal transduction and endocytosis: close encounters of many kinds. Nat Rev Mol Cell Biol 2002, 3:600-614.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 600-614
    • Sorkin, A.1    Von Zastrow, M.2
  • 15
  • 16
    • 3142523461 scopus 로고    scopus 로고
    • COP and clathrin-coated vesicle budding: different pathways, common approaches
    • McMahon H.T., Mills I.G. COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr Opin Cell Biol 2004, 16:379-391.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 379-391
    • McMahon, H.T.1    Mills, I.G.2
  • 17
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner S.D., Schmid S.L. Regulated portals of entry into the cell. Nature 2003, 422:37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 18
    • 64249153782 scopus 로고    scopus 로고
    • Ready, set, internalize: mechanisms and regulation of GLUT4 endocytosis
    • Antonescu C.N., Foti M., Sauvonnet N., Klip A. Ready, set, internalize: mechanisms and regulation of GLUT4 endocytosis. Biosci Rep 2009, 29:1-11.
    • (2009) Biosci Rep , vol.29 , pp. 1-11
    • Antonescu, C.N.1    Foti, M.2    Sauvonnet, N.3    Klip, A.4
  • 19
    • 34547969807 scopus 로고    scopus 로고
    • Endocytosis: clathrin-mediated membrane budding
    • Ungewickell E.J., Hinrichsen L. Endocytosis: clathrin-mediated membrane budding. Curr Opin Cell Biol 2007, 19:417-425.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 417-425
    • Ungewickell, E.J.1    Hinrichsen, L.2
  • 20
    • 12144262710 scopus 로고    scopus 로고
    • Cortactin and dynamin are required for the clathrin-independent endocytosis of gamma c cytokine receptor
    • Sauvonnet N., Dujeancourt A., Dautry-Varsat A. Cortactin and dynamin are required for the clathrin-independent endocytosis of gamma c cytokine receptor. J Cell Biol 2005, 168:155-163.
    • (2005) J Cell Biol , vol.168 , pp. 155-163
    • Sauvonnet, N.1    Dujeancourt, A.2    Dautry-Varsat, A.3
  • 21
    • 33846615966 scopus 로고    scopus 로고
    • The neck of caveolae is a distinct plasma membrane subdomain that concentrates insulin receptors in 3T3-L1 adipocytes
    • Foti M., Porcheron G., Fournier M., Maeder C., Carpentier J.L. The neck of caveolae is a distinct plasma membrane subdomain that concentrates insulin receptors in 3T3-L1 adipocytes. Proc Natl Acad Sci U S A 2007, 104:1242-1247.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1242-1247
    • Foti, M.1    Porcheron, G.2    Fournier, M.3    Maeder, C.4    Carpentier, J.L.5
  • 24
    • 35648978204 scopus 로고    scopus 로고
    • Caveolin-1 regulates the delivery and endocytosis of the glutamate transporter, excitatory amino acid carrier 1
    • Gonzalez M.I., Krizman-Genda E., Robinson M.B. Caveolin-1 regulates the delivery and endocytosis of the glutamate transporter, excitatory amino acid carrier 1. J Biol Chem 2007, 282:29855-29865.
    • (2007) J Biol Chem , vol.282 , pp. 29855-29865
    • Gonzalez, M.I.1    Krizman-Genda, E.2    Robinson, M.B.3
  • 25
    • 24944555198 scopus 로고    scopus 로고
    • The glycosphingolipid, lactosylceramide, regulates beta1-integrin clustering and endocytosis
    • Sharma D.K., Brown J.C., Cheng Z., Holicky E.L., Marks D.L., Pagano R.E. The glycosphingolipid, lactosylceramide, regulates beta1-integrin clustering and endocytosis. Cancer Res 2005, 65:8233-8241.
    • (2005) Cancer Res , vol.65 , pp. 8233-8241
    • Sharma, D.K.1    Brown, J.C.2    Cheng, Z.3    Holicky, E.L.4    Marks, D.L.5    Pagano, R.E.6
  • 27
    • 0033280324 scopus 로고    scopus 로고
    • Adaptors for clathrin-mediated traffic
    • Kirchhausen T. Adaptors for clathrin-mediated traffic. Annu Rev Cell Dev Biol 1999, 15:705-732.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 705-732
    • Kirchhausen, T.1
  • 29
    • 34247357880 scopus 로고    scopus 로고
    • Dileucine motif is sufficient for internalization and synaptic vesicle targeting of vesicular acetylcholine transporter
    • Colgan L., Liu H., Huang S.Y., Liu Y.J. Dileucine motif is sufficient for internalization and synaptic vesicle targeting of vesicular acetylcholine transporter. Traffic 2007, 8:512-522.
    • (2007) Traffic , vol.8 , pp. 512-522
    • Colgan, L.1    Liu, H.2    Huang, S.Y.3    Liu, Y.J.4
  • 30
    • 0026772733 scopus 로고
    • A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains
    • Letourneur F., Klausner R.D. A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains. Cell 1992, 69:1143-1157.
    • (1992) Cell , vol.69 , pp. 1143-1157
    • Letourneur, F.1    Klausner, R.D.2
  • 32
    • 0026806542 scopus 로고
    • A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor is necessary for the lysosomal enzyme sorting function
    • Johnson K.F., Kornfeld S. A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor is necessary for the lysosomal enzyme sorting function. J Biol Chem 1992, 267:17110-17115.
    • (1992) J Biol Chem , vol.267 , pp. 17110-17115
    • Johnson, K.F.1    Kornfeld, S.2
  • 35
    • 46349107416 scopus 로고    scopus 로고
    • Value of combining activated brain FDG-PET and cardiac MIBG for the differential diagnosis of dementia: differentiation of dementia with Lewy bodies and Alzheimer disease when the diagnoses based on clinical and neuroimaging criteria are difficult
    • Schmidt S.L., Correa P.L., Tolentino J.C., Manhaes A.C., Felix R.M., Azevedo J.C., Barbirato G.B., Mendes M.H., Boechat Y., Cabral H., et al. Value of combining activated brain FDG-PET and cardiac MIBG for the differential diagnosis of dementia: differentiation of dementia with Lewy bodies and Alzheimer disease when the diagnoses based on clinical and neuroimaging criteria are difficult. Clin Nucl Med 2008, 33:398-401.
    • (2008) Clin Nucl Med , vol.33 , pp. 398-401
    • Schmidt, S.L.1    Correa, P.L.2    Tolentino, J.C.3    Manhaes, A.C.4    Felix, R.M.5    Azevedo, J.C.6    Barbirato, G.B.7    Mendes, M.H.8    Boechat, Y.9    Cabral, H.10
  • 36
    • 1542274278 scopus 로고    scopus 로고
    • Glucose transporter GLUT8 translocation in neurons is not insulin responsive
    • Shin B.C., McKnight R.A., Devaskar S.U. Glucose transporter GLUT8 translocation in neurons is not insulin responsive. J Neurosci Res 2004, 75:835-844.
    • (2004) J Neurosci Res , vol.75 , pp. 835-844
    • Shin, B.C.1    McKnight, R.A.2    Devaskar, S.U.3
  • 37
    • 33745509798 scopus 로고    scopus 로고
    • Endocytosis of the glucose transporter GLUT8 is mediated by interaction of a dileucine motif with the beta2-adaptin subunit of the AP-2 adaptor complex
    • Schmidt U., Briese S., Leicht K., Schurmann A., Joost H.G., Al-Hasani H. Endocytosis of the glucose transporter GLUT8 is mediated by interaction of a dileucine motif with the beta2-adaptin subunit of the AP-2 adaptor complex. J Cell Sci 2006, 119:2321-2331.
    • (2006) J Cell Sci , vol.119 , pp. 2321-2331
    • Schmidt, U.1    Briese, S.2    Leicht, K.3    Schurmann, A.4    Joost, H.G.5    Al-Hasani, H.6
  • 38
    • 0346102461 scopus 로고    scopus 로고
    • Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes
    • Janvier K., Kato Y., Boehm M., Rose J.R., Martina J.A., Kim B.Y., Venkatesan S., Bonifacino J.S. Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes. J Cell Biol 2003, 163:1281-1290.
    • (2003) J Cell Biol , vol.163 , pp. 1281-1290
    • Janvier, K.1    Kato, Y.2    Boehm, M.3    Rose, J.R.4    Martina, J.A.5    Kim, B.Y.6    Venkatesan, S.7    Bonifacino, J.S.8
  • 39
    • 0039252786 scopus 로고    scopus 로고
    • The leucine-based sorting motifs in the cytoplasmic domain of the invariant chain are recognized by the clathrin adaptors AP1 and AP2 and their medium chains
    • Hofmann M.W., Honing S., Rodionov D., Dobberstein B., von Figura K., Bakke O. The leucine-based sorting motifs in the cytoplasmic domain of the invariant chain are recognized by the clathrin adaptors AP1 and AP2 and their medium chains. J Biol Chem 1999, 274:36153-36158.
    • (1999) J Biol Chem , vol.274 , pp. 36153-36158
    • Hofmann, M.W.1    Honing, S.2    Rodionov, D.3    Dobberstein, B.4    von Figura, K.5    Bakke, O.6
  • 40
    • 33645240278 scopus 로고    scopus 로고
    • High density lipoprotein endocytosis by scavenger receptor SR-BII is clathrin-dependent and requires a carboxyl-terminal dileucine motif
    • Eckhardt E.R., Cai L., Shetty S., Zhao Z., Szanto A., Webb N.R., Van der Westhuyzen D.R. High density lipoprotein endocytosis by scavenger receptor SR-BII is clathrin-dependent and requires a carboxyl-terminal dileucine motif. J Biol Chem 2006, 281:4348-4353.
    • (2006) J Biol Chem , vol.281 , pp. 4348-4353
    • Eckhardt, E.R.1    Cai, L.2    Shetty, S.3    Zhao, Z.4    Szanto, A.5    Webb, N.R.6    Van der Westhuyzen, D.R.7
  • 41
    • 33745513790 scopus 로고    scopus 로고
    • Identification of endophilins 1 and 3 as selective binding partners for VGLUT1 and their co-localization in neocortical glutamatergic synapses: implications for vesicular glutamate transporter trafficking and excitatory vesicle formation
    • De Gois S., Jeanclos E., Morris M., Grewal S., Varoqui H., Erickson J.D. Identification of endophilins 1 and 3 as selective binding partners for VGLUT1 and their co-localization in neocortical glutamatergic synapses: implications for vesicular glutamate transporter trafficking and excitatory vesicle formation. Cell Mol Neurobiol 2006, 26:679-693.
    • (2006) Cell Mol Neurobiol , vol.26 , pp. 679-693
    • De Gois, S.1    Jeanclos, E.2    Morris, M.3    Grewal, S.4    Varoqui, H.5    Erickson, J.D.6
  • 42
    • 33745494172 scopus 로고    scopus 로고
    • Distinct endocytic pathways control the rate and extent of synaptic vesicle protein recycling
    • Voglmaier S.M., Kam K., Yang H., Fortin D.L., Hua Z., Nicoll R.A., Edwards R.H. Distinct endocytic pathways control the rate and extent of synaptic vesicle protein recycling. Neuron 2006, 51:71-84.
    • (2006) Neuron , vol.51 , pp. 71-84
    • Voglmaier, S.M.1    Kam, K.2    Yang, H.3    Fortin, D.L.4    Hua, Z.5    Nicoll, R.A.6    Edwards, R.H.7
  • 43
    • 33645713636 scopus 로고    scopus 로고
    • Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface
    • Choudhury A., Marks D.L., Proctor K.M., Gould G.W., Pagano R.E. Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface. Nat Cell Biol 2006, 8:317-328.
    • (2006) Nat Cell Biol , vol.8 , pp. 317-328
    • Choudhury, A.1    Marks, D.L.2    Proctor, K.M.3    Gould, G.W.4    Pagano, R.E.5
  • 44
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP2 complex
    • Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J. Molecular architecture and functional model of the endocytic AP2 complex. Cell 2002, 109:523-535.
    • (2002) Cell , vol.109 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 45
    • 1842832338 scopus 로고    scopus 로고
    • Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit
    • Yao D., Ehrlich M., Henis Y.I., Leof E.B. Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit. Mol Biol Cell 2002, 13:4001-4012.
    • (2002) Mol Biol Cell , vol.13 , pp. 4001-4012
    • Yao, D.1    Ehrlich, M.2    Henis, Y.I.3    Leof, E.B.4
  • 46
    • 34248198351 scopus 로고    scopus 로고
    • The gamma/sigma1 and alpha/sigma2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site
    • Doray B., Lee I., Knisely J., Bu G., Kornfeld S. The gamma/sigma1 and alpha/sigma2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site. Mol Biol Cell 2007, 18:1887-1896.
    • (2007) Mol Biol Cell , vol.18 , pp. 1887-1896
    • Doray, B.1    Lee, I.2    Knisely, J.3    Bu, G.4    Kornfeld, S.5
  • 47
    • 57749196168 scopus 로고    scopus 로고
    • A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex
    • Kelly B.T., McCoy A.J., Spate K., Miller S.E., Evans P.R., Honing S., Owen D.J. A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex. Nature 2008, 456:976-979.
    • (2008) Nature , vol.456 , pp. 976-979
    • Kelly, B.T.1    McCoy, A.J.2    Spate, K.3    Miller, S.E.4    Evans, P.R.5    Honing, S.6    Owen, D.J.7
  • 48
    • 0037062410 scopus 로고    scopus 로고
    • Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif
    • Doray B., Bruns K., Ghosh P., Kornfeld S.A. Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif. Proc Natl Acad Sci U S A 2002, 99:8072-8077.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 8072-8077
    • Doray, B.1    Bruns, K.2    Ghosh, P.3    Kornfeld, S.A.4
  • 49
    • 0035158494 scopus 로고    scopus 로고
    • Adaptins: the final recount
    • Boehm M., Bonifacino J.S. Adaptins: the final recount. Mol Biol Cell 2001, 12:2907-2920.
    • (2001) Mol Biol Cell , vol.12 , pp. 2907-2920
    • Boehm, M.1    Bonifacino, J.S.2
  • 50
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: adaptors on the move
    • Bonifacino J.S. The GGA proteins: adaptors on the move. Nat Rev Mol Cell Biol 2004, 5:23-32.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 23-32
    • Bonifacino, J.S.1
  • 51
    • 26244449833 scopus 로고    scopus 로고
    • A novel dileucine lysosomal-sorting-signal mediates intracellular EGF-receptor retention independently of protein ubiquitylation
    • Tsacoumangos A., Kil S.J., Ma L., Sonnichsen F.D., Carlin C. A novel dileucine lysosomal-sorting-signal mediates intracellular EGF-receptor retention independently of protein ubiquitylation. J Cell Sci 2005, 118:3959-3971.
    • (2005) J Cell Sci , vol.118 , pp. 3959-3971
    • Tsacoumangos, A.1    Kil, S.J.2    Ma, L.3    Sonnichsen, F.D.4    Carlin, C.5
  • 52
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen W.J., Goldstein J.L., Brown M.S. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J Biol Chem 1990, 265:3116-3123.
    • (1990) J Biol Chem , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 53
    • 0022456630 scopus 로고
    • The J.D. mutation in familial hypercholesterolemia: amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors
    • Davis C.G., Lehrman M.A., Russell D.W., Anderson R.G., Brown M.S., Goldstein J.L. The J.D. mutation in familial hypercholesterolemia: amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors. Cell 1986, 45:15-24.
    • (1986) Cell , vol.45 , pp. 15-24
    • Davis, C.G.1    Lehrman, M.A.2    Russell, D.W.3    Anderson, R.G.4    Brown, M.S.5    Goldstein, J.L.6
  • 54
    • 35648951623 scopus 로고    scopus 로고
    • A NPxY-independent beta5 integrin activation signal regulates phagocytosis of apoptotic cells
    • Singh S., D'Mello V., van Bergen en Henegouwen P., Birge R.B. A NPxY-independent beta5 integrin activation signal regulates phagocytosis of apoptotic cells. Biochem Biophys Res Commun 2007, 364:540-548.
    • (2007) Biochem Biophys Res Commun , vol.364 , pp. 540-548
    • Singh, S.1    D'Mello, V.2    van Bergen en Henegouwen, P.3    Birge, R.B.4
  • 55
    • 41149103877 scopus 로고    scopus 로고
    • NPXY motifs in the beta1 integrin cytoplasmic tail are required for functional reovirus entry
    • Maginnis M.S., Mainou B.A., Derdowski A., Johnson E.M., Zent R., Dermody T.S. NPXY motifs in the beta1 integrin cytoplasmic tail are required for functional reovirus entry. J Virol 2008, 82:3181-3191.
    • (2008) J Virol , vol.82 , pp. 3181-3191
    • Maginnis, M.S.1    Mainou, B.A.2    Derdowski, A.3    Johnson, E.M.4    Zent, R.5    Dermody, T.S.6
  • 58
    • 33644864081 scopus 로고    scopus 로고
    • Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization
    • Paing M.M., Johnston C.A., Siderovski D.P., Trejo J. Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization. Mol Cell Biol 2006, 26:3231-3242.
    • (2006) Mol Cell Biol , vol.26 , pp. 3231-3242
    • Paing, M.M.1    Johnston, C.A.2    Siderovski, D.P.3    Trejo, J.4
  • 59
    • 0242330147 scopus 로고    scopus 로고
    • Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection
    • Traub L.M. Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection. J Cell Biol 2003, 163:203-208.
    • (2003) J Cell Biol , vol.163 , pp. 203-208
    • Traub, L.M.1
  • 60
    • 0035099375 scopus 로고    scopus 로고
    • Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2
    • Morris S.M., Cooper J.A. Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2. Traffic 2001, 2:111-123.
    • (2001) Traffic , vol.2 , pp. 111-123
    • Morris, S.M.1    Cooper, J.A.2
  • 61
    • 0034193309 scopus 로고    scopus 로고
    • Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin
    • Oleinikov A.V., Zhao J., Makker S.P. Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin. Biochem J 2000, 347(Pt 3):613-621.
    • (2000) Biochem J , vol.347 , Issue.PART 3 , pp. 613-621
    • Oleinikov, A.V.1    Zhao, J.2    Makker, S.P.3
  • 62
    • 0032514158 scopus 로고    scopus 로고
    • The LDL receptor clustering motif interacts with the clathrin terminal domain in a reverse turn conformation
    • Kibbey R.G., Rizo J., Gierasch L.M., Anderson R.G. The LDL receptor clustering motif interacts with the clathrin terminal domain in a reverse turn conformation. J Cell Biol 1998, 142:59-67.
    • (1998) J Cell Biol , vol.142 , pp. 59-67
    • Kibbey, R.G.1    Rizo, J.2    Gierasch, L.M.3    Anderson, R.G.4
  • 63
    • 0026040579 scopus 로고
    • Transplanted LDL and mannose-6-phosphate receptor internalization signals promote high-efficiency endocytosis of the transferrin receptor
    • Collawn J.F., Kuhn L.A., Liu L.F., Tainer J.A., Trowbridge I.S. Transplanted LDL and mannose-6-phosphate receptor internalization signals promote high-efficiency endocytosis of the transferrin receptor. EMBO J 1991, 10:3247-3253.
    • (1991) EMBO J , vol.10 , pp. 3247-3253
    • Collawn, J.F.1    Kuhn, L.A.2    Liu, L.F.3    Tainer, J.A.4    Trowbridge, I.S.5
  • 64
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42
    • Perez R.G., Soriano S., Hayes J.D., Ostaszewski B., Xia W., Selkoe D.J., Chen X., Stokin G.B., Koo E.H. Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42. J Biol Chem 1999, 274:18851-18856.
    • (1999) J Biol Chem , vol.274 , pp. 18851-18856
    • Perez, R.G.1    Soriano, S.2    Hayes, J.D.3    Ostaszewski, B.4    Xia, W.5    Selkoe, D.J.6    Chen, X.7    Stokin, G.B.8    Koo, E.H.9
  • 65
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni R., Rice D.S., Sheldon M., Curran T. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J Neurosci 1999, 19:7507-7515.
    • (1999) J Neurosci , vol.19 , pp. 7507-7515
    • Homayouni, R.1    Rice, D.S.2    Sheldon, M.3    Curran, T.4
  • 66
    • 0035997373 scopus 로고    scopus 로고
    • Lipoprotein receptors in the nervous system
    • Herz J., Bock H.H. Lipoprotein receptors in the nervous system. Annu Rev Biochem 2002, 71:405-434.
    • (2002) Annu Rev Biochem , vol.71 , pp. 405-434
    • Herz, J.1    Bock, H.H.2
  • 67
    • 0037113960 scopus 로고    scopus 로고
    • ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2
    • He G., Gupta S., Yi M., Michaely P., Hobbs H.H., Cohen J.C. ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2. J Biol Chem 2002, 277:44044-44049.
    • (2002) J Biol Chem , vol.277 , pp. 44044-44049
    • He, G.1    Gupta, S.2    Yi, M.3    Michaely, P.4    Hobbs, H.H.5    Cohen, J.C.6
  • 68
    • 0037339887 scopus 로고    scopus 로고
    • Grb2 regulates internalization of EGF receptors through clathrin-coated pits
    • Jiang X., Huang F., Marusyk A., Sorkin A. Grb2 regulates internalization of EGF receptors through clathrin-coated pits. Mol Biol Cell 2003, 14:858-870.
    • (2003) Mol Biol Cell , vol.14 , pp. 858-870
    • Jiang, X.1    Huang, F.2    Marusyk, A.3    Sorkin, A.4
  • 70
    • 0037009042 scopus 로고    scopus 로고
    • Integrin activation takes shape
    • Liddington R.C., Ginsberg M.H. Integrin activation takes shape. J Cell Biol 2002, 158:833-839.
    • (2002) J Cell Biol , vol.158 , pp. 833-839
    • Liddington, R.C.1    Ginsberg, M.H.2
  • 71
    • 19544384364 scopus 로고    scopus 로고
    • Internalization and trafficking of guanylyl (guanylate) cyclase/natriuretic peptide receptor A is regulated by an acidic tyrosine-based cytoplasmic motif GDAY
    • Pandey K.N., Nguyen H.T., Garg R., Khurana M.L., Fink J. Internalization and trafficking of guanylyl (guanylate) cyclase/natriuretic peptide receptor A is regulated by an acidic tyrosine-based cytoplasmic motif GDAY. Biochem J 2005, 388:103-113.
    • (2005) Biochem J , vol.388 , pp. 103-113
    • Pandey, K.N.1    Nguyen, H.T.2    Garg, R.3    Khurana, M.L.4    Fink, J.5
  • 72
    • 21044443474 scopus 로고    scopus 로고
    • Neuronal Ca2+ sensor protein VILIP-1 affects cGMP signalling of guanylyl cyclase B by regulating clathrin-dependent receptor recycling in hippocampal neurons
    • Brackmann M., Schuchmann S., Anand R., Braunewell K.H. Neuronal Ca2+ sensor protein VILIP-1 affects cGMP signalling of guanylyl cyclase B by regulating clathrin-dependent receptor recycling in hippocampal neurons. J Cell Sci 2005, 118:2495-2505.
    • (2005) J Cell Sci , vol.118 , pp. 2495-2505
    • Brackmann, M.1    Schuchmann, S.2    Anand, R.3    Braunewell, K.H.4
  • 73
    • 75049085850 scopus 로고    scopus 로고
    • Analysis of natriuretic peptide receptor A internalization by ribonucleic acid interference
    • Somanna N.K., Arise K.K., Pandey K.N. Analysis of natriuretic peptide receptor A internalization by ribonucleic acid interference. J Am Investig Med 2007, 55:S262.
    • (2007) J Am Investig Med , vol.55
    • Somanna, N.K.1    Arise, K.K.2    Pandey, K.N.3
  • 74
    • 0036510758 scopus 로고    scopus 로고
    • Agonist-induced internalization of the platelet-activating factor receptor is dependent on arrestins but independent of G-protein activation. Role of the C terminus and the (D/N)PXXY motif
    • Chen Z., Dupre D.J., Le Gouill C., Rola-Pleszczynski M., Stankova J. Agonist-induced internalization of the platelet-activating factor receptor is dependent on arrestins but independent of G-protein activation. Role of the C terminus and the (D/N)PXXY motif. J Biol Chem 2002, 277:7356-7362.
    • (2002) J Biol Chem , vol.277 , pp. 7356-7362
    • Chen, Z.1    Dupre, D.J.2    Le Gouill, C.3    Rola-Pleszczynski, M.4    Stankova, J.5
  • 76
    • 0034595799 scopus 로고    scopus 로고
    • The YXXL motif, but not the two NPXY motifs, serves as the dominant endocytosis signal for low density lipoprotein receptor-related protein
    • Li Y., Marzolo M.P., van Kerkhof P., Strous G.J., Bu G. The YXXL motif, but not the two NPXY motifs, serves as the dominant endocytosis signal for low density lipoprotein receptor-related protein. J Biol Chem 2000, 275:17187-17194.
    • (2000) J Biol Chem , vol.275 , pp. 17187-17194
    • Li, Y.1    Marzolo, M.P.2    van Kerkhof, P.3    Strous, G.J.4    Bu, G.5
  • 77
    • 0025635559 scopus 로고
    • Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis
    • Collawn J.F., Stangel M., Kuhn L.A., Esekogwu V., Jing S.Q., Trowbridge I.S., Tainer J.A. Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis. Cell 1990, 63:1061-1072.
    • (1990) Cell , vol.63 , pp. 1061-1072
    • Collawn, J.F.1    Stangel, M.2    Kuhn, L.A.3    Esekogwu, V.4    Jing, S.Q.5    Trowbridge, I.S.6    Tainer, J.A.7
  • 78
    • 0025037001 scopus 로고
    • Characteristics of the tyrosine recognition signal for internalization of transmembrane surface glycoproteins
    • Ktistakis N.T., Thomas D., Roth M.G. Characteristics of the tyrosine recognition signal for internalization of transmembrane surface glycoproteins. J Cell Biol 1990, 111:1393-1407.
    • (1990) J Cell Biol , vol.111 , pp. 1393-1407
    • Ktistakis, N.T.1    Thomas, D.2    Roth, M.G.3
  • 79
    • 0026342565 scopus 로고
    • The essential tyrosine of the internalization signal in lysosomal acid phosphatase is part of a beta turn
    • Eberle W., Sander C., Klaus W., Schmidt B., von Figura K., Peters C. The essential tyrosine of the internalization signal in lysosomal acid phosphatase is part of a beta turn. Cell 1991, 67:1203-1209.
    • (1991) Cell , vol.67 , pp. 1203-1209
    • Eberle, W.1    Sander, C.2    Klaus, W.3    Schmidt, B.4    von Figura, K.5    Peters, C.6
  • 80
    • 0035192658 scopus 로고    scopus 로고
    • GGAs: roles of the different domains and comparison with AP-1 and clathrin
    • Hirst J., Lindsay M.R., Robinson M.S. GGAs: roles of the different domains and comparison with AP-1 and clathrin. Mol Biol Cell 2001, 12:3573-3588.
    • (2001) Mol Biol Cell , vol.12 , pp. 3573-3588
    • Hirst, J.1    Lindsay, M.R.2    Robinson, M.S.3
  • 81
    • 0035831509 scopus 로고    scopus 로고
    • Role of the differentially spliced carboxyl terminus in thromboxane A2 receptor trafficking: identification of a distinct motif for tonic internalization
    • Parent J.L., Labrecque P., Driss Rochdi M., Benovic J.L. Role of the differentially spliced carboxyl terminus in thromboxane A2 receptor trafficking: identification of a distinct motif for tonic internalization. J Biol Chem 2001, 276:7079-7085.
    • (2001) J Biol Chem , vol.276 , pp. 7079-7085
    • Parent, J.L.1    Labrecque, P.2    Driss Rochdi, M.3    Benovic, J.L.4
  • 83
    • 0033491059 scopus 로고    scopus 로고
    • Utilization of the indirect lysosome targeting pathway by lysosome-associated membrane proteins (LAMPs) is influenced largely by the C-terminal residue of their GYXXphi targeting signals
    • Gough N.R., Zweifel M.E., Martinez-Augustin O., Aguilar R.C., Bonifacino J.S., Fambrough D.M. Utilization of the indirect lysosome targeting pathway by lysosome-associated membrane proteins (LAMPs) is influenced largely by the C-terminal residue of their GYXXphi targeting signals. J Cell Sci 1999, 112(Pt 23):4257-4269.
    • (1999) J Cell Sci , vol.112 , Issue.PART 23 , pp. 4257-4269
    • Gough, N.R.1    Zweifel, M.E.2    Martinez-Augustin, O.3    Aguilar, R.C.4    Bonifacino, J.S.5    Fambrough, D.M.6
  • 84
    • 0026545549 scopus 로고
    • Transport of the lysosomal membrane glycoprotein lgp120 (lgp-A) to lysosomes does not require appearance on the plasma membrane
    • Harter C., Mellman I. Transport of the lysosomal membrane glycoprotein lgp120 (lgp-A) to lysosomes does not require appearance on the plasma membrane. J Cell Biol 1992, 117:311-325.
    • (1992) J Cell Biol , vol.117 , pp. 311-325
    • Harter, C.1    Mellman, I.2
  • 85
    • 0029670902 scopus 로고    scopus 로고
    • The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane
    • Rohrer J., Schweizer A., Russell D., Kornfeld S. The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. J Cell Biol 1996, 132:565-576.
    • (1996) J Cell Biol , vol.132 , pp. 565-576
    • Rohrer, J.1    Schweizer, A.2    Russell, D.3    Kornfeld, S.4
  • 86
    • 0029826535 scopus 로고    scopus 로고
    • Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains
    • Ohno H., Fournier M.C., Poy G., Bonifacino J.S. Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains. J Biol Chem 1996, 271:29009-29015.
    • (1996) J Biol Chem , vol.271 , pp. 29009-29015
    • Ohno, H.1    Fournier, M.C.2    Poy, G.3    Bonifacino, J.S.4
  • 87
    • 45549098590 scopus 로고    scopus 로고
    • The chemokine receptor CXCR3 is degraded following internalization and is replenished at the cell surface by de novo synthesis of receptor
    • Meiser A., Mueller A., Wise E.L., McDonagh E.M., Petit S.J., Saran N., Clark P.C., Williams T.J., Pease J.E. The chemokine receptor CXCR3 is degraded following internalization and is replenished at the cell surface by de novo synthesis of receptor. J Immunol 2008, 180:6713-6724.
    • (2008) J Immunol , vol.180 , pp. 6713-6724
    • Meiser, A.1    Mueller, A.2    Wise, E.L.3    McDonagh, E.M.4    Petit, S.J.5    Saran, N.6    Clark, P.C.7    Williams, T.J.8    Pease, J.E.9
  • 88
    • 33744960879 scopus 로고    scopus 로고
    • A C-terminal lysine that controls human P2X4 receptor desensitization
    • Fountain S.J., North R.A. A C-terminal lysine that controls human P2X4 receptor desensitization. J Biol Chem 2006, 281:15044-15049.
    • (2006) J Biol Chem , vol.281 , pp. 15044-15049
    • Fountain, S.J.1    North, R.A.2
  • 89
    • 0034441994 scopus 로고    scopus 로고
    • Surface expression of Kv1 voltage-gated K+ channels is governed by a C-terminal motif
    • Levitan E.S., Takimoto K. Surface expression of Kv1 voltage-gated K+ channels is governed by a C-terminal motif. Trends Cardiovasc Med 2000, 10:317-320.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 317-320
    • Levitan, E.S.1    Takimoto, K.2
  • 90
    • 0034823954 scopus 로고    scopus 로고
    • Identification of two distinct structural motifs that, when added to the C-terminal tail of the rat LH receptor, redirect the internalized hormone-receptor complex from a degradation to a recycling pathway
    • Kishi M., Liu X., Hirakawa T., Reczek D., Bretscher A., Ascoli M. Identification of two distinct structural motifs that, when added to the C-terminal tail of the rat LH receptor, redirect the internalized hormone-receptor complex from a degradation to a recycling pathway. Mol Endocrinol 2001, 15:1624-1635.
    • (2001) Mol Endocrinol , vol.15 , pp. 1624-1635
    • Kishi, M.1    Liu, X.2    Hirakawa, T.3    Reczek, D.4    Bretscher, A.5    Ascoli, M.6
  • 91
    • 0034744184 scopus 로고    scopus 로고
    • Differential effect of GalNAcalpha-O-bn on intracellular trafficking in enterocytic HT-29 and Caco-2 cells: correlation with the glycosyltransferase expression pattern
    • Gouyer V., Leteurtre E., Delmotte P., Steelant W.F., Krzewinski-Recchi M.A., Zanetta J.P., Lesuffleur T., Trugnan G., Delannoy P., Huet G. Differential effect of GalNAcalpha-O-bn on intracellular trafficking in enterocytic HT-29 and Caco-2 cells: correlation with the glycosyltransferase expression pattern. J Cell Sci 2001, 114:1455-1471.
    • (2001) J Cell Sci , vol.114 , pp. 1455-1471
    • Gouyer, V.1    Leteurtre, E.2    Delmotte, P.3    Steelant, W.F.4    Krzewinski-Recchi, M.A.5    Zanetta, J.P.6    Lesuffleur, T.7    Trugnan, G.8    Delannoy, P.9    Huet, G.10
  • 92
    • 17544383706 scopus 로고    scopus 로고
    • A di-hydrophobic Leu-Val motif regulates the basolateral localization of CD44 in polarized Madin-Darby canine kidney epithelial cells
    • Sheikh H., Isacke C.M. A di-hydrophobic Leu-Val motif regulates the basolateral localization of CD44 in polarized Madin-Darby canine kidney epithelial cells. J Biol Chem 1996, 271:12185-12190.
    • (1996) J Biol Chem , vol.271 , pp. 12185-12190
    • Sheikh, H.1    Isacke, C.M.2
  • 93
    • 0027956397 scopus 로고
    • Hyaluronate receptors: key players in growth, differentiation, migration and tumor progression
    • Sherman L., Sleeman J., Herrlich P., Ponta H. Hyaluronate receptors: key players in growth, differentiation, migration and tumor progression. Curr Opin Cell Biol 1994, 6:726-733.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 726-733
    • Sherman, L.1    Sleeman, J.2    Herrlich, P.3    Ponta, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.