메뉴 건너뛰기




Volumn 39, Issue , 2016, Pages 53-60

Signal processing by the endosomal system

Author keywords

[No Author keywords available]

Indexed keywords

BIODIVERSITY; CELL FATE; CELL INTERACTION; CELL KINETICS; CELL MIGRATION; DIGITAL COMPUTER; ENDOCYTOSIS; ENDOSOME; INTERNALIZATION; LIGAND BINDING; PRIORITY JOURNAL; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION; ANIMAL; HUMAN; KINETICS; METABOLISM; TRANSPORT AT THE CELLULAR LEVEL;

EID: 84958972786     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2016.02.002     Document Type: Review
Times cited : (127)

References (67)
  • 1
    • 80052047534 scopus 로고    scopus 로고
    • Information theory based approaches to cellular signaling
    • Waltermann C., Klipp E. Information theory based approaches to cellular signaling. Biochim Biophys Acta 2011, 1810:924-932.
    • (2011) Biochim Biophys Acta , vol.1810 , pp. 924-932
    • Waltermann, C.1    Klipp, E.2
  • 2
    • 84940644968 scopus 로고
    • A mathematical theory of communication
    • Shannon C. A mathematical theory of communication. Bell Syst Tech J 1948, 27:379-423.
    • (1948) Bell Syst Tech J , vol.27 , pp. 379-423
    • Shannon, C.1
  • 3
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: hubs for controlling the flow of cellular information
    • Good M.C., Zalatan J.G., Lim W.A. Scaffold proteins: hubs for controlling the flow of cellular information. Science 2011, 332:680-686.
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 4
    • 78951489049 scopus 로고    scopus 로고
    • Feedback regulation of EGFR signalling: decision making by early and delayed loops
    • Avraham R., Yarden Y. Feedback regulation of EGFR signalling: decision making by early and delayed loops. Nat Rev Mol Cell Biol 2011, 12:104-117.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 104-117
    • Avraham, R.1    Yarden, Y.2
  • 5
    • 63749113783 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: thirty years and counting
    • Hunter T. Tyrosine phosphorylation: thirty years and counting. Curr Opin Cell Biol 2009, 21:140-146.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 140-146
    • Hunter, T.1
  • 6
    • 84894460034 scopus 로고    scopus 로고
    • When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling
    • Nguyen L.K., Kolch W., Kholodenko B.N. When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling. Cell Commun Signal 2013, 11:52.
    • (2013) Cell Commun Signal , vol.11 , pp. 52
    • Nguyen, L.K.1    Kolch, W.2    Kholodenko, B.N.3
  • 7
    • 84922393807 scopus 로고    scopus 로고
    • Ubiquitination in disease pathogenesis and treatment
    • Popovic D., Vucic D., Dikic I. Ubiquitination in disease pathogenesis and treatment. Nat Med 2014, 20:1242-1253.
    • (2014) Nat Med , vol.20 , pp. 1242-1253
    • Popovic, D.1    Vucic, D.2    Dikic, I.3
  • 8
    • 73849105365 scopus 로고    scopus 로고
    • SUMOylation and cell signalling
    • Andreou A.M., Tavernarakis N. SUMOylation and cell signalling. Biotechnol J 2009, 4:1740-1752.
    • (2009) Biotechnol J , vol.4 , pp. 1740-1752
    • Andreou, A.M.1    Tavernarakis, N.2
  • 9
    • 84872824241 scopus 로고    scopus 로고
    • Design principles of regulatory networks: searching for the molecular algorithms of the cell
    • Lim W.A., Lee C.M., Tang C. Design principles of regulatory networks: searching for the molecular algorithms of the cell. Mol Cell 2013, 49:202-212.
    • (2013) Mol Cell , vol.49 , pp. 202-212
    • Lim, W.A.1    Lee, C.M.2    Tang, C.3
  • 10
    • 33847355217 scopus 로고    scopus 로고
    • Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate
    • Santos S.D.M., Verveer P.J., Bastiaens P.I.H. Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate. Nat Cell Biol 2007, 9:324-330.
    • (2007) Nat Cell Biol , vol.9 , pp. 324-330
    • Santos, S.D.M.1    Verveer, P.J.2    Bastiaens, P.I.H.3
  • 12
    • 84887191269 scopus 로고    scopus 로고
    • Effects of membrane trafficking on signaling by receptor tyrosine kinases
    • Miaczynska M. Effects of membrane trafficking on signaling by receptor tyrosine kinases. Cold Spring Harb Perspect Biol 2013, 5:a009035.
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , pp. a009035
    • Miaczynska, M.1
  • 13
    • 3142592401 scopus 로고    scopus 로고
    • Not just a sink: endosomes in control of signal transduction
    • Miaczynska M., Pelkmans L., Zerial M. Not just a sink: endosomes in control of signal transduction. Curr Opin Cell Biol 2004, 16:400-406.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 400-406
    • Miaczynska, M.1    Pelkmans, L.2    Zerial, M.3
  • 19
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink J., Ghigo E., Kalaidzidis Y., Zerial M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 2005, 122:735-749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 20
    • 84929483072 scopus 로고    scopus 로고
    • Rab proteins and the compartmentalization of the endosomal system
    • Wandinger-Ness A., Zerial M. Rab proteins and the compartmentalization of the endosomal system. Cold Spring Harb Perspect Biol 2014, 6:a022616.
    • (2014) Cold Spring Harb Perspect Biol , vol.6 , pp. a022616
    • Wandinger-Ness, A.1    Zerial, M.2
  • 22
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial M., McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001, 2:107-117.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 26
    • 62549151303 scopus 로고    scopus 로고
    • A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes
    • Zoncu R., Perera R.M., Balkin D.M., Pirruccello M., Toomre D., De Camilli P. A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes. Cell 2009, 136:1110-1121.
    • (2009) Cell , vol.136 , pp. 1110-1121
    • Zoncu, R.1    Perera, R.M.2    Balkin, D.M.3    Pirruccello, M.4    Toomre, D.5    De Camilli, P.6
  • 27
    • 84858665104 scopus 로고    scopus 로고
    • Suppression of EGFR endocytosis by dynamin depletion reveals that EGFR signaling occurs primarily at the plasma membrane
    • Sousa L.P., Lax I., Shen H., Ferguson S.M., Camilli P.D., Schlessinger J. Suppression of EGFR endocytosis by dynamin depletion reveals that EGFR signaling occurs primarily at the plasma membrane. Proc Natl Acad Sci 2012, 109:4419-4424.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 4419-4424
    • Sousa, L.P.1    Lax, I.2    Shen, H.3    Ferguson, S.M.4    Camilli, P.D.5    Schlessinger, J.6
  • 29
    • 0029134736 scopus 로고
    • Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin
    • Damke H., Baba T., van der Bliek A.M., Schmid S.L. Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin. J Cell Biol 1995, 131:69-80.
    • (1995) J Cell Biol , vol.131 , pp. 69-80
    • Damke, H.1    Baba, T.2    van der Bliek, A.M.3    Schmid, S.L.4
  • 30
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • Di Guglielmo G.M., Baass P.C., Ou W.J., Posner B.I., Bergeron J.J. Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J 1994, 13:4269-4277.
    • (1994) EMBO J , vol.13 , pp. 4269-4277
    • Di Guglielmo, G.M.1    Baass, P.C.2    Ou, W.J.3    Posner, B.I.4    Bergeron, J.J.5
  • 31
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira A.V., Lamaze C., Schmid S.L. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 1996, 274:2086-2089.
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 32
    • 84892496733 scopus 로고    scopus 로고
    • Live-cell fluorescence imaging reveals high stoichiometry of Grb2 binding to the EGF receptor sustained during endocytosis
    • Fortian A., Sorkin A. Live-cell fluorescence imaging reveals high stoichiometry of Grb2 binding to the EGF receptor sustained during endocytosis. J Cell Sci 2014, 127:432-444.
    • (2014) J Cell Sci , vol.127 , pp. 432-444
    • Fortian, A.1    Sorkin, A.2
  • 33
    • 84901020430 scopus 로고    scopus 로고
    • Receptor tyrosine kinase c-Met controls the cytoskeleton from different endosomes via different pathways
    • Ménard L., Parker P.J., Kermorgant S. Receptor tyrosine kinase c-Met controls the cytoskeleton from different endosomes via different pathways. Nat Commun 2014, 5:3907.
    • (2014) Nat Commun , vol.5 , pp. 3907
    • Ménard, L.1    Parker, P.J.2    Kermorgant, S.3
  • 35
    • 84964694996 scopus 로고    scopus 로고
    • Regulation of EGFR signal transduction by analogue-to-digital conversion in endosomes
    • Villaseñor R., Nonaka H., Del Conte-Zerial P., Kalaidzidis Y., Zerial M. Regulation of EGFR signal transduction by analogue-to-digital conversion in endosomes. Elife 2015, 4:1-32.
    • (2015) Elife , vol.4 , pp. 1-32
    • Villaseñor, R.1    Nonaka, H.2    Del Conte-Zerial, P.3    Kalaidzidis, Y.4    Zerial, M.5
  • 37
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev B., Ong S.-E., Kratchmarova I., Mann M. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat Biotechnol 2004, 22:1139-1145.
    • (2004) Nat Biotechnol , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.-E.2    Kratchmarova, I.3    Mann, M.4
  • 38
    • 84865599600 scopus 로고    scopus 로고
    • Endosomal crosstalk: meeting points for signaling pathways
    • Pálfy M., Reményi A., Korcsmáros T. Endosomal crosstalk: meeting points for signaling pathways. Trends Cell Biol 2012, 22:447-456.
    • (2012) Trends Cell Biol , vol.22 , pp. 447-456
    • Pálfy, M.1    Reményi, A.2    Korcsmáros, T.3
  • 39
    • 84938908176 scopus 로고    scopus 로고
    • PYK2 sustains endosomal-derived receptor signalling and enhances epithelial-to-mesenchymal transition
    • Verma N., Keinan O., Selitrennik M., Karn T., Filipits M., Lev S. PYK2 sustains endosomal-derived receptor signalling and enhances epithelial-to-mesenchymal transition. Nat Commun 2015, 6:6064.
    • (2015) Nat Commun , vol.6 , pp. 6064
    • Verma, N.1    Keinan, O.2    Selitrennik, M.3    Karn, T.4    Filipits, M.5    Lev, S.6
  • 41
    • 58249105213 scopus 로고    scopus 로고
    • APPL1: role in adiponectin signaling and beyond
    • Deepa S.S., Dong L.Q. APPL1: role in adiponectin signaling and beyond. Am J Physiol Endocrinol Metab 2009, 296:E22-E36.
    • (2009) Am J Physiol Endocrinol Metab , vol.296 , pp. E22-E36
    • Deepa, S.S.1    Dong, L.Q.2
  • 42
    • 84869099031 scopus 로고    scopus 로고
    • APPL1 regulates basal NF-κB activity by stabilizing NIK
    • Hupalowska A., Pyrzynska B., Miaczynska M. APPL1 regulates basal NF-κB activity by stabilizing NIK. J Cell Sci 2012, 125:4090-4102.
    • (2012) J Cell Sci , vol.125 , pp. 4090-4102
    • Hupalowska, A.1    Pyrzynska, B.2    Miaczynska, M.3
  • 43
    • 79951849928 scopus 로고    scopus 로고
    • An APPL1/Akt signaling complex regulates dendritic spine and synapse formation in hippocampal neurons
    • Majumdar D., Nebhan C.A., Hu L., Anderson B., Webb D.J. An APPL1/Akt signaling complex regulates dendritic spine and synapse formation in hippocampal neurons. Mol Cell Neurosci 2011, 46:633-644.
    • (2011) Mol Cell Neurosci , vol.46 , pp. 633-644
    • Majumdar, D.1    Nebhan, C.A.2    Hu, L.3    Anderson, B.4    Webb, D.J.5
  • 44
    • 42949092018 scopus 로고    scopus 로고
    • The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development
    • Schenck A., Goto-Silva L., Collinet C., Rhinn M., Giner A., Habermann B., Brand M., Zerial M. The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development. Cell 2008, 133:486-497.
    • (2008) Cell , vol.133 , pp. 486-497
    • Schenck, A.1    Goto-Silva, L.2    Collinet, C.3    Rhinn, M.4    Giner, A.5    Habermann, B.6    Brand, M.7    Zerial, M.8
  • 45
    • 78650795768 scopus 로고    scopus 로고
    • APPL1 mediates adiponectin-stimulated p38 MAPK activation by scaffolding the TAK1-MKK3-p38 MAPK pathway
    • Xin X., Zhou L., Reyes C.M., Liu F., Dong L.Q. APPL1 mediates adiponectin-stimulated p38 MAPK activation by scaffolding the TAK1-MKK3-p38 MAPK pathway. Am J Physiol Endocrinol Metab 2011, 300:E103-E110.
    • (2011) Am J Physiol Endocrinol Metab , vol.300 , pp. E103-E110
    • Xin, X.1    Zhou, L.2    Reyes, C.M.3    Liu, F.4    Dong, L.Q.5
  • 46
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • Haj F.G., Verveer P.J., Squire A., Neel B.G., Bastiaens P.I.H. Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 2002, 295:1708-1711.
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.H.5
  • 47
    • 77649274212 scopus 로고    scopus 로고
    • Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction
    • Eden E.R., White I.J., Tsapara A., Futter C.E. Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction. Nat Cell Biol 2010, 12:267-272.
    • (2010) Nat Cell Biol , vol.12 , pp. 267-272
    • Eden, E.R.1    White, I.J.2    Tsapara, A.3    Futter, C.E.4
  • 48
    • 84939839414 scopus 로고    scopus 로고
    • Ubiquitination switches EphA2 vesicular traffic from a continuous safeguard to a finite signalling mode
    • Sabet O., Stockert R., Xouri G., Brüggemann Y., Stanoev A., Bastiaens P.I.H. Ubiquitination switches EphA2 vesicular traffic from a continuous safeguard to a finite signalling mode. Nat Commun 2015, 6:8047.
    • (2015) Nat Commun , vol.6 , pp. 8047
    • Sabet, O.1    Stockert, R.2    Xouri, G.3    Brüggemann, Y.4    Stanoev, A.5    Bastiaens, P.I.H.6
  • 49
  • 52
    • 84923141003 scopus 로고    scopus 로고
    • Ras nanoclusters: versatile lipid-based signaling platforms
    • Zhou Y., Hancock J.F. Ras nanoclusters: versatile lipid-based signaling platforms. Biochim Biophys Acta 2015, 1853:841-849.
    • (2015) Biochim Biophys Acta , vol.1853 , pp. 841-849
    • Zhou, Y.1    Hancock, J.F.2
  • 53
    • 77955825161 scopus 로고    scopus 로고
    • Spatial organization of transmembrane receptor signalling
    • Bethani I., Skånland S.S., Dikic I., Acker-Palmer A. Spatial organization of transmembrane receptor signalling. EMBO J 2010, 29:2677-2688.
    • (2010) EMBO J , vol.29 , pp. 2677-2688
    • Bethani, I.1    Skånland, S.S.2    Dikic, I.3    Acker-Palmer, A.4
  • 54
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X., Gureasko J., Shen K., Cole P.A., Kuriyan J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 2006, 125:1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 55
    • 79952672026 scopus 로고    scopus 로고
    • Signaling from the living plasma membrane
    • Grecco H.E., Schmick M., Bastiaens P.I.H. Signaling from the living plasma membrane. Cell 2011, 144:897-909.
    • (2011) Cell , vol.144 , pp. 897-909
    • Grecco, H.E.1    Schmick, M.2    Bastiaens, P.I.H.3
  • 56
    • 0142059890 scopus 로고    scopus 로고
    • Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling
    • Agazie Y.M., Hayman M.J. Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling. Mol Cell Biol 2003, 23:7875-7886.
    • (2003) Mol Cell Biol , vol.23 , pp. 7875-7886
    • Agazie, Y.M.1    Hayman, M.J.2
  • 57
    • 0002011401 scopus 로고
    • The Chemical Basis of Morphogenesis
    • Turing A.M. The Chemical Basis of Morphogenesis. Philos Trans R Soc B Biol Sci 1952, 237:37-72.
    • (1952) Philos Trans R Soc B Biol Sci , vol.237 , pp. 37-72
    • Turing, A.M.1
  • 58
    • 69249137477 scopus 로고    scopus 로고
    • Endocytosis and signalling: intertwining molecular networks
    • Sorkin A., von Zastrow M. Endocytosis and signalling: intertwining molecular networks. Nat Rev Mol Cell Biol 2009, 10:609-622.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 609-622
    • Sorkin, A.1    von Zastrow, M.2
  • 59
    • 84879987829 scopus 로고    scopus 로고
    • AKT facilitates EGFR trafficking and degradation by phosphorylating and activating PIKfyve
    • Er E.E., Mendoza M.C., Mackey A.M., Rameh L.E., Blenis J. AKT facilitates EGFR trafficking and degradation by phosphorylating and activating PIKfyve. Sci Signal 2013, 6:ra45.
    • (2013) Sci Signal , vol.6 , pp. ra45
    • Er, E.E.1    Mendoza, M.C.2    Mackey, A.M.3    Rameh, L.E.4    Blenis, J.5
  • 60
    • 25144481466 scopus 로고    scopus 로고
    • Phosphorylation of EEA1 by p38 MAP kinase regulates mu opioid receptor endocytosis
    • Macé G., Miaczynska M., Zerial M., Nebreda A.R. Phosphorylation of EEA1 by p38 MAP kinase regulates mu opioid receptor endocytosis. EMBO J 2005, 24:3235-3246.
    • (2005) EMBO J , vol.24 , pp. 3235-3246
    • Macé, G.1    Miaczynska, M.2    Zerial, M.3    Nebreda, A.R.4
  • 61
    • 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
  • 62
    • 70349466529 scopus 로고    scopus 로고
    • Population context determines cell-to-cell variability in endocytosis and virus infection
    • Snijder B., Sacher R., Rämö P., Damm E.-M., Liberali P., Pelkmans L. Population context determines cell-to-cell variability in endocytosis and virus infection. Nature 2009, 461:520-523.
    • (2009) Nature , vol.461 , pp. 520-523
    • Snijder, B.1    Sacher, R.2    Rämö, P.3    Damm, E.-M.4    Liberali, P.5    Pelkmans, L.6
  • 65
    • 51649130231 scopus 로고    scopus 로고
    • Receptor trafficking controls weak signal delivery: a strategy used by c-Met for STAT3 nuclear accumulation
    • Kermorgant S., Parker P.J. Receptor trafficking controls weak signal delivery: a strategy used by c-Met for STAT3 nuclear accumulation. J Cell Biol 2008, 182:855-863.
    • (2008) J Cell Biol , vol.182 , pp. 855-863
    • Kermorgant, S.1    Parker, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.