-
1
-
-
0036902646
-
Receptor downregulation and multivesicular-body sorting
-
This article highlights the physiological roles of multivesicular endosomes (MVEs) and gives a comprehensive overview of the molecular mechanisms involved in receptor sorting and MVE formation, with a special focus on the role of ubiquitin, ubiquitin-binding proteins and ESCRT complexes.
-
Katzmann D.J., Odorizzi G., Emr S.D. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3:2002;893-905 This article highlights the physiological roles of multivesicular endosomes (MVEs) and gives a comprehensive overview of the molecular mechanisms involved in receptor sorting and MVE formation, with a special focus on the role of ubiquitin, ubiquitin-binding proteins and ESCRT complexes.
-
(2002)
Nat. Rev. Mol. Cell Biol.
, vol.3
, pp. 893-905
-
-
Katzmann, D.J.1
Odorizzi, G.2
Emr, S.D.3
-
2
-
-
0036481624
-
Secretory lysosomes
-
This review discusses the biogenesis of and sorting into secretory lysosomes, and further how secretory lysosomes can undergo regulated exocytosis.
-
Blott E.J., Griffiths G.M. Secretory lysosomes. Nat. Rev. Mol. Cell Biol. 3:2002;122-131 This review discusses the biogenesis of and sorting into secretory lysosomes, and further how secretory lysosomes can undergo regulated exocytosis.
-
(2002)
Nat. Rev. Mol. Cell Biol.
, vol.3
, pp. 122-131
-
-
Blott, E.J.1
Griffiths, G.M.2
-
5
-
-
0035823004
-
Argosomes: A potential vehicle for the spread of morphogens through epithelia
-
Greco V., Hannus M., Eaton S. Argosomes: a potential vehicle for the spread of morphogens through epithelia. Cell. 106:2001;633-645.
-
(2001)
Cell
, vol.106
, pp. 633-645
-
-
Greco, V.1
Hannus, M.2
Eaton, S.3
-
6
-
-
0035823032
-
A new ticket for entry into budding vesicles - Ubiquitin
-
Hicke L. A new ticket for entry into budding vesicles - ubiquitin. Cell. 106:2001;527-530.
-
(2001)
Cell
, vol.106
, pp. 527-530
-
-
Hicke, L.1
-
7
-
-
0034768447
-
Involvement of the ubiquitin/proteasome system in sorting of the interleukin 2 receptor beta chain to late endocytic compartments
-
Rocca A., Lamaze C., Subtil A., Dautry-Varsat A. Involvement of the ubiquitin/proteasome system in sorting of the interleukin 2 receptor beta chain to late endocytic compartments. Mol. Biol. Cell. 12:2001;1293-1301.
-
(2001)
Mol. Biol. Cell
, vol.12
, pp. 1293-1301
-
-
Rocca, A.1
Lamaze, C.2
Subtil, A.3
Dautry-Varsat, A.4
-
8
-
-
0035824563
-
Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting
-
Marchese A., Benovic J.L. Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting. J. Biol. Chem. 276:2001;45509-45512.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 45509-45512
-
-
Marchese, A.1
Benovic, J.L.2
-
9
-
-
0035834428
-
Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin
-
Shenoy S.K., McDonald P.H., Kohout T.A., Lefkowitz R.J. Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin. Science. 294:2001;1307-1313.
-
(2001)
Science
, vol.294
, pp. 1307-1313
-
-
Shenoy, S.K.1
McDonald, P.H.2
Kohout, T.A.3
Lefkowitz, R.J.4
-
10
-
-
0034235434
-
Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
-
Rotin D., Staub O., Haguenauer-Tsapis R. Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J. Membr. Biol. 176:2000;1-17.
-
(2000)
J. Membr. Biol.
, vol.176
, pp. 1-17
-
-
Rotin, D.1
Staub, O.2
Haguenauer-Tsapis, R.3
-
11
-
-
0034852403
-
Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
-
Urbanowski J.L., Piper R.C. Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole. Traffic. 2:2001;622-630.
-
(2001)
Traffic
, vol.2
, pp. 622-630
-
-
Urbanowski, J.L.1
Piper, R.C.2
-
12
-
-
0035903635
-
Sorting of proteins into multivesicular bodies: Ubiquitin-dependent and -independent targeting
-
Reggiori F., Pelham H.R. Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting. EMBO J. 20:2001;5176-5186.
-
(2001)
EMBO J.
, vol.20
, pp. 5176-5186
-
-
Reggiori, F.1
Pelham, H.R.2
-
13
-
-
0036094538
-
Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes
-
d is estimated to be in the high micromolar range. By studying a transferrin receptor that has been recombinantly fused with ubiquitin, this report provides evidence that Hrs can recognise ubiquitinated cargo and retain it in the endosomal bilayered Hrs/clathrin coat, thereby preventing recycling.
-
d is estimated to be in the high micromolar range. By studying a transferrin receptor that has been recombinantly fused with ubiquitin, this report provides evidence that Hrs can recognise ubiquitinated cargo and retain it in the endosomal bilayered Hrs/clathrin coat, thereby preventing recycling.
-
(2002)
Nat. Cell Biol.
, vol.4
, pp. 394-398
-
-
Raiborg, C.1
Bache, K.G.2
Gillooly, D.J.3
Madshus, I.H.4
Stang, E.5
Stenmark, H.6
-
14
-
-
0035369556
-
A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems
-
Hofmann K., Falquet L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem. Sci. 26:2001;347-350.
-
(2001)
Trends Biochem. Sci.
, vol.26
, pp. 347-350
-
-
Hofmann, K.1
Falquet, L.2
-
15
-
-
0037169336
-
Hrs regulates endosome invagination and receptor tyrosine kinase signaling in Drosophila
-
Germline mutant embryos that lack full-length Hrs protein die early in embryogenesis, whereas zygotic mutants make it to the third-instar larvae/early pupae stage, probably owing to long-lived, maternally deposited Hrs. Hrs mutant larvae have enlarged endosomes, owing to an inability of endosomes to invaginate their limiting membrane, and hence a reduction in the number of multivesicular endosomes (MVEs) is observed. Hrs mutant embryos have increased activation and signalling from epidermal growth factor and Torso receptors, suggesting that trafficking into MVEs plays an important role in signal attenuation.
-
Lloyd T.E., Atkinson R., Wu M.N., Zhou Y., Pennetta G., Bellen H.J. Hrs regulates endosome invagination and receptor tyrosine kinase signaling in Drosophila. Cell. 108:2002;261-269 Germline mutant embryos that lack full-length Hrs protein die early in embryogenesis, whereas zygotic mutants make it to the third-instar larvae/early pupae stage, probably owing to long-lived, maternally deposited Hrs. Hrs mutant larvae have enlarged endosomes, owing to an inability of endosomes to invaginate their limiting membrane, and hence a reduction in the number of multivesicular endosomes (MVEs) is observed. Hrs mutant embryos have increased activation and signalling from epidermal growth factor and Torso receptors, suggesting that trafficking into MVEs plays an important role in signal attenuation.
-
(2002)
Cell
, vol.108
, pp. 261-269
-
-
Lloyd, T.E.1
Atkinson, R.2
Wu, M.N.3
Zhou, Y.4
Pennetta, G.5
Bellen, H.J.6
-
16
-
-
0037518120
-
The yeast epsin Ent1 is recruited to membranes through multiple independent interactions
-
Aguilar R.C., Watson H.A., Wendland B. The yeast epsin Ent1 is recruited to membranes through multiple independent interactions. J. Biol. Chem. 278:2003;10737-10743.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 10737-10743
-
-
Aguilar, R.C.1
Watson, H.A.2
Wendland, B.3
-
17
-
-
0036544559
-
Mammalian class E Vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates
-
This report shows that ubiquitinated proteins accumulate on epidermal growth factor (EGF)-containing endosomes in EGF-stimulated cells, together with mammalian class E proteins such as Tsg101 and hVps28. These proteins, in addition to Hrs, are further shown to interact with ubiquitin. Microinjection of anti-hVps28 antibodies or depletion of Tsg101 by small interfering RNA cause ubiquitinated proteins to accumulate on endosomes and retard EGF degradation.
-
Bishop N., Horman A., Woodman P. Mammalian class E Vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. J. Cell Biol. 157:2002;91-101 This report shows that ubiquitinated proteins accumulate on epidermal growth factor (EGF)-containing endosomes in EGF-stimulated cells, together with mammalian class E proteins such as Tsg101 and hVps28. These proteins, in addition to Hrs, are further shown to interact with ubiquitin. Microinjection of anti-hVps28 antibodies or depletion of Tsg101 by small interfering RNA cause ubiquitinated proteins to accumulate on endosomes and retard EGF degradation.
-
(2002)
J. Cell Biol.
, vol.157
, pp. 91-101
-
-
Bishop, N.1
Horman, A.2
Woodman, P.3
-
18
-
-
0036304360
-
The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting
-
Co-immunoprecipitation experiments indicate that Vps27p and Hse1p form a complex, and both proteins are pulled down from yeast cell lysates using ubiquitin beads. Mutations in the ubiquitin-interacting motif of both proteins result in specific defects in the sorting of ubiquitinated proteins into the vacuole lumen.
-
Bilodeau P.S., Urbanowski J.L., Winistorfer S.C., Piper R.C. The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat. Cell Biol. 4:2002;534-539 Co-immunoprecipitation experiments indicate that Vps27p and Hse1p form a complex, and both proteins are pulled down from yeast cell lysates using ubiquitin beads. Mutations in the ubiquitin-interacting motif of both proteins result in specific defects in the sorting of ubiquitinated proteins into the vacuole lumen.
-
(2002)
Nat. Cell Biol.
, vol.4
, pp. 534-539
-
-
Bilodeau, P.S.1
Urbanowski, J.L.2
Winistorfer, S.C.3
Piper, R.C.4
-
19
-
-
0036094688
-
Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
-
The interaction between ubiquitin- and ubiquitin-interacting motif (UIM)-containing proteins is characterised; Ile44 of ubiquitin is critical for its ability to bind UIMs. Whereas Epsin UIMs are important for internalisation of monoubiquitinated receptors from the plasma membrane, Vps27 UIMs are necessary to sort endocytic and biosynthetic cargo into the multivesicular endosome pathway.
-
Shih S.C., Katzmann D.J., Schnell J.D., Sutanto M., Emr S.D., Hicke L. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 4:2002;389-393 The interaction between ubiquitin- and ubiquitin-interacting motif (UIM)-containing proteins is characterised; Ile44 of ubiquitin is critical for its ability to bind UIMs. Whereas Epsin UIMs are important for internalisation of monoubiquitinated receptors from the plasma membrane, Vps27 UIMs are necessary to sort endocytic and biosynthetic cargo into the multivesicular endosome pathway.
-
(2002)
Nat. Cell Biol.
, vol.4
, pp. 389-393
-
-
Shih, S.C.1
Katzmann, D.J.2
Schnell, J.D.3
Sutanto, M.4
Emr, S.D.5
Hicke, L.6
-
20
-
-
0037187597
-
A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
-
Several endocytic proteins, such as Hrs, Eps15 and Epsins, are monoubiquitinated in EGF-stimulated cells, and a functional ubiquitin-interacting motif (UIM) is required for this modification. The authors predict the existence of a UIM-/ubiquitin-based network of endocytic proteins and ubiquitinated cargo.
-
Polo S., Sigismund S., Faretta M., Guidi M., Capua M.R., Bossi G., Chen H., De Camilli P., Di Fiore P.P. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature. 416:2002;451-455 Several endocytic proteins, such as Hrs, Eps15 and Epsins, are monoubiquitinated in EGF-stimulated cells, and a functional ubiquitin-interacting motif (UIM) is required for this modification. The authors predict the existence of a UIM-/ubiquitin-based network of endocytic proteins and ubiquitinated cargo.
-
(2002)
Nature
, vol.416
, pp. 451-455
-
-
Polo, S.1
Sigismund, S.2
Faretta, M.3
Guidi, M.4
Capua, M.R.5
Bossi, G.6
Chen, H.7
De Camilli, P.8
Di Fiore, P.P.9
-
21
-
-
0038323973
-
STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
-
Bache K.G., Raiborg C., Mehlum A., Stenmark H. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278:2003;12513-12521.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 12513-12521
-
-
Bache, K.G.1
Raiborg, C.2
Mehlum, A.3
Stenmark, H.4
-
22
-
-
18544383164
-
Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4
-
Katz M., Shtiegman K., Tal-Or P., Yakir L., Mosesson Y., Harari D., Machluf Y., Asao H., Jovin T., Sugamura K., Yarden Y. Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic. 3:2002;740-751.
-
(2002)
Traffic
, vol.3
, pp. 740-751
-
-
Katz, M.1
Shtiegman, K.2
Tal-Or, P.3
Yakir, L.4
Mosesson, Y.5
Harari, D.6
Machluf, Y.7
Asao, H.8
Jovin, T.9
Sugamura, K.10
Yarden, Y.11
-
23
-
-
0037093316
-
Structure and functional interactions of the Tsg101 UEV domain
-
This study continues the story of the role of Tsg101 in vacuolar protein sorting and virus budding recently published by the same group [55]. By resolving the structure of the Tsg101 UEV (ubiquitin-binding) domain and providing chemical shift mapping of the ubiquitin- and PTAP-binding sites, this report gives insight into how Tsg101 can act in these processes.
-
Pornillos O., Alam S.L., Rich R.L., Myszka D.G., Davis D.R., Sundquist W.I. Structure and functional interactions of the Tsg101 UEV domain. EMBO J. 21:2002;2397-2406 This study continues the story of the role of Tsg101 in vacuolar protein sorting and virus budding recently published by the same group [55]. By resolving the structure of the Tsg101 UEV (ubiquitin-binding) domain and providing chemical shift mapping of the ubiquitin- and PTAP-binding sites, this report gives insight into how Tsg101 can act in these processes.
-
(2002)
EMBO J.
, vol.21
, pp. 2397-2406
-
-
Pornillos, O.1
Alam, S.L.2
Rich, R.L.3
Myszka, D.G.4
Davis, D.R.5
Sundquist, W.I.6
-
24
-
-
0035958546
-
Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
-
Katzmann D.J., Babst M., Emr S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell. 106:2001;145-155.
-
(2001)
Cell
, vol.106
, pp. 145-155
-
-
Katzmann, D.J.1
Babst, M.2
Emr, S.D.3
-
25
-
-
0036902815
-
Epsins: Adaptors in endocytosis?
-
Wendland B. Epsins: adaptors in endocytosis? Nat. Rev. Mol. Cell Biol. 3:2002;971-977.
-
(2002)
Nat. Rev. Mol. Cell Biol.
, vol.3
, pp. 971-977
-
-
Wendland, B.1
-
26
-
-
0036231098
-
Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes
-
This report shows beautiful electron microscopy (EM) images of the endosomal clathrin/Hrs coat. The authors suggest a role for this coat in lysosomal protein sorting. Quantitative immuno-EM shows that the lysosomal targeted growth hormone receptor and the epidermal growth factor receptor are concentrated in the coat, whereas the recycling transferrin receptor is not.
-
Sachse M., Urbé S., Oorschot V., Strous G.J., Klumperman J. Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes. Mol. Biol. Cell. 13:2002;1313-1328 This report shows beautiful electron microscopy (EM) images of the endosomal clathrin/Hrs coat. The authors suggest a role for this coat in lysosomal protein sorting. Quantitative immuno-EM shows that the lysosomal targeted growth hormone receptor and the epidermal growth factor receptor are concentrated in the coat, whereas the recycling transferrin receptor is not.
-
(2002)
Mol. Biol. Cell
, vol.13
, pp. 1313-1328
-
-
Sachse, M.1
Urbé, S.2
Oorschot, V.3
Strous, G.J.4
Klumperman, J.5
-
27
-
-
0035801478
-
Hrs recruits clathrin to early endosomes
-
Raiborg C., Bache K.G., Mehlum A., Stang E., Stenmark H. Hrs recruits clathrin to early endosomes. EMBO J. 20:2001;5008-5021.
-
(2001)
EMBO J.
, vol.20
, pp. 5008-5021
-
-
Raiborg, C.1
Bache, K.G.2
Mehlum, A.3
Stang, E.4
Stenmark, H.5
-
28
-
-
0035854827
-
Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
-
Dunn R., Hicke L. Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J. Biol. Chem. 276:2001;25974-25981.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 25974-25981
-
-
Dunn, R.1
Hicke, L.2
-
29
-
-
0035941194
-
Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1
-
Soetens O., De Craene J.O., Andre B. Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J. Biol. Chem. 276:2001;43949-43957.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 43949-43957
-
-
Soetens, O.1
De Craene, J.O.2
Andre, B.3
-
30
-
-
0036166924
-
A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies
-
This report identifies a Golgi-associated transmembrane ubiquitin ligase, Tul1, which induces ubiquitination and multivesicular endosome sorting of proteins with polar residues exposed in their transmembrane domains. The authors suggest that this serves as a quality control to degrade incorrectly folded membrane proteins in the vacuole.
-
Reggiori F., Pelham H.R. A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies. Nat. Cell Biol. 4:2002;117-123 This report identifies a Golgi-associated transmembrane ubiquitin ligase, Tul1, which induces ubiquitination and multivesicular endosome sorting of proteins with polar residues exposed in their transmembrane domains. The authors suggest that this serves as a quality control to degrade incorrectly folded membrane proteins in the vacuole.
-
(2002)
Nat. Cell Biol.
, vol.4
, pp. 117-123
-
-
Reggiori, F.1
Pelham, H.R.2
-
31
-
-
0037154292
-
Protein degradation: Four E3s for the Notch pathway
-
This review summarises studies in C. elegans, Drosophila and mouse reported in 2001 showing the roles of four E3 ubiquitin ligases involved in Notch-Delta signalling. Suppressor of Deltex/Itch is a negative regulator of Notch-Delta signalling and is able to ubiquinate Notch. Sel-10 is another negative regulator of Notch, promoting its ubiquination and degradation. Neuralised is a regulator of Notch-Delta signalling, which binds, monoubiquinates and promotes degradation of Delta. LNX promotes ubiquination and degradation of the Numb PTB domain protein, a regulator of Notch-Delta signalling.
-
Lai E.C. Protein degradation: four E3s for the Notch pathway. Curr. Biol. 12:2002;R74-R78 This review summarises studies in C. elegans, Drosophila and mouse reported in 2001 showing the roles of four E3 ubiquitin ligases involved in Notch-Delta signalling. Suppressor of Deltex/Itch is a negative regulator of Notch-Delta signalling and is able to ubiquinate Notch. Sel-10 is another negative regulator of Notch, promoting its ubiquination and degradation. Neuralised is a regulator of Notch-Delta signalling, which binds, monoubiquinates and promotes degradation of Delta. LNX promotes ubiquination and degradation of the Numb PTB domain protein, a regulator of Notch-Delta signalling.
-
(2002)
Curr. Biol.
, vol.12
-
-
Lai, E.C.1
-
32
-
-
0035651380
-
Drosophila neuralized is a ubiquitin ligase that promotes the internalization and degradation of Delta
-
Lai E.C., Deblandre G.A., Kintner C., Rubin G.M. Drosophila neuralized is a ubiquitin ligase that promotes the internalization and degradation of Delta. Dev. Cell. 1:2001;783-794.
-
(2001)
Dev. Cell
, vol.1
, pp. 783-794
-
-
Lai, E.C.1
Deblandre, G.A.2
Kintner, C.3
Rubin, G.M.4
-
33
-
-
0035650895
-
Xenopus neuralized is a ubiquitin ligase that interacts with XDelta1 and regulates Notch signaling
-
Deblandre G.A., Lai E.C., Kintner C. Xenopus neuralized is a ubiquitin ligase that interacts with XDelta1 and regulates Notch signaling. Dev. Cell. 1:2001;795-806.
-
(2001)
Dev. Cell
, vol.1
, pp. 795-806
-
-
Deblandre, G.A.1
Lai, E.C.2
Kintner, C.3
-
34
-
-
0035653308
-
Neuralized encodes a peripheral membrane protein involved in delta signaling and endocytosis
-
Pavlopoulos E., Pitsouli C., Klueg K.M., Muskavitch M.A., Moschonas N.K., Delidakis C. Neuralized encodes a peripheral membrane protein involved in delta signaling and endocytosis. Dev. Cell. 1:2001;807-816.
-
(2001)
Dev. Cell
, vol.1
, pp. 807-816
-
-
Pavlopoulos, E.1
Pitsouli, C.2
Klueg, K.M.3
Muskavitch, M.A.4
Moschonas, N.K.5
Delidakis, C.6
-
35
-
-
0037238008
-
Mind bomb is a ubiquitin ligase that is essential for efficient activation of notch signaling by delta
-
Positional cloning of a gene necessary for Notch-Delta signalling in zebrafish led to the identification of a gene encoding an E3 RING-finger ubiquitin ligase, termed 'Mind Bomb' (Mib). Biochemical and co-expression experiments in COS7 cells revealed that Mib binds several Delta homologues and promotes their ubiquitination and internalisation, and that they co-localise on a Rab9-labelled endocytic compartment. Interestingly the increased internalisation of Delta promotes Notch activation, suggesting that Delta internalisation might be required to make Delta an effective ligand.
-
Itoh M., Kim C.H., Palardy G., Oda T., Jiang Y.J., Maust D., Yeo S.Y., Lorick K., Wright G.J., Ariza-McNaughton L.et al. Mind bomb is a ubiquitin ligase that is essential for efficient activation of notch signaling by delta. Dev. Cell. 4:2003;67-82 Positional cloning of a gene necessary for Notch-Delta signalling in zebrafish led to the identification of a gene encoding an E3 RING-finger ubiquitin ligase, termed 'Mind Bomb' (Mib). Biochemical and co-expression experiments in COS7 cells revealed that Mib binds several Delta homologues and promotes their ubiquitination and internalisation, and that they co-localise on a Rab9-labelled endocytic compartment. Interestingly the increased internalisation of Delta promotes Notch activation, suggesting that Delta internalisation might be required to make Delta an effective ligand.
-
(2003)
Dev. Cell
, vol.4
, pp. 67-82
-
-
Itoh, M.1
Kim, C.H.2
Palardy, G.3
Oda, T.4
Jiang, Y.J.5
Maust, D.6
Yeo, S.Y.7
Lorick, K.8
Wright, G.J.9
Ariza-McNaughton, L.10
-
36
-
-
0032217156
-
C-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
-
Levkowitz G., Waterman H., Zamir E., Kam Z., Oved S., Langdon W.Y., Beguinot L., Geiger B., Yarden Y. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12:1998;3663-3674.
-
(1998)
Genes Dev.
, vol.12
, pp. 3663-3674
-
-
Levkowitz, G.1
Waterman, H.2
Zamir, E.3
Kam, Z.4
Oved, S.5
Langdon, W.Y.6
Beguinot, L.7
Geiger, B.8
Yarden, Y.9
-
37
-
-
0034864712
-
The ubiquitin-proteasome pathway regulates lysosomal degradation of the growth hormone receptor and its ligand
-
Van Kerkhof P., Strous G.J. The ubiquitin-proteasome pathway regulates lysosomal degradation of the growth hormone receptor and its ligand. Biochem. Soc. Trans. 29:2001;488-493.
-
(2001)
Biochem. Soc. Trans.
, vol.29
, pp. 488-493
-
-
Van Kerkhof, P.1
Strous, G.J.2
-
38
-
-
0035159679
-
Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins
-
Van Kerkhof P., dos Santos C.M., Sachse M., Klumperman J., Bu G., Strous G.J. Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins. Mol. Biol. Cell. 12:2001;2556-2566.
-
(2001)
Mol. Biol. Cell
, vol.12
, pp. 2556-2566
-
-
Van Kerkhof, P.1
Dos Santos, C.M.2
Sachse, M.3
Klumperman, J.4
Bu, G.5
Strous, G.J.6
-
39
-
-
0036732911
-
Proteasome regulates the delivery of LDL receptor-related protein into the degradation pathway
-
Proteasome inhibitors inhibit endocytic downregulation of both the growth hormone receptor and the epidermal growth factor receptor. This report gives another example of a receptor that requires the ubiquitin-proteasome system for lysosomal degradation. Instead of being sorted into multivesicular endosomes, the low-density lipoprotein receptor related protein is recycled back to the plasma membrane in the presence of proteasomal inhibitors.
-
Melman L., Geuze H.J., Li Y., McCormick L.M., Van Kerkhof P., Strous G.J., Schwartz A.L., Bu G. Proteasome regulates the delivery of LDL receptor-related protein into the degradation pathway. Mol. Biol. Cell. 13:2002;3325-3335 Proteasome inhibitors inhibit endocytic downregulation of both the growth hormone receptor and the epidermal growth factor receptor. This report gives another example of a receptor that requires the ubiquitin-proteasome system for lysosomal degradation. Instead of being sorted into multivesicular endosomes, the low-density lipoprotein receptor related protein is recycled back to the plasma membrane in the presence of proteasomal inhibitors.
-
(2002)
Mol. Biol. Cell
, vol.13
, pp. 3325-3335
-
-
Melman, L.1
Geuze, H.J.2
Li, Y.3
McCormick, L.M.4
Van Kerkhof, P.5
Strous, G.J.6
Schwartz, A.L.7
Bu, G.8
-
40
-
-
0037018146
-
Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies
-
Epidermal growth factor (EGF) induces EGF receptor (EGFR) downregulation, whereas another EGFR-ligand, transforming growth factor α, does not. The EGFR is ubiquitinated upon stimulation with both ligands, but the ubiquitination is sustained when stimulating with EGF. EGF stimulation also leads to the recruitment of the ubiquitin ligase c-Cbl to EGFR-positive endosomes. Proteasome inhibitors are shown to inhibit the sorting of ubiquitinated EGFR into multivesicular endosomes.
-
Longva K.E., Blystad F.D., Stang E., Larsen A.M., Johannessen L.E., Madshus I.H. Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies. J. Cell Biol. 156:2002;843-854 Epidermal growth factor (EGF) induces EGF receptor (EGFR) downregulation, whereas another EGFR-ligand, transforming growth factor α, does not. The EGFR is ubiquitinated upon stimulation with both ligands, but the ubiquitination is sustained when stimulating with EGF. EGF stimulation also leads to the recruitment of the ubiquitin ligase c-Cbl to EGFR-positive endosomes. Proteasome inhibitors are shown to inhibit the sorting of ubiquitinated EGFR into multivesicular endosomes.
-
(2002)
J. Cell Biol.
, vol.156
, pp. 843-854
-
-
Longva, K.E.1
Blystad, F.D.2
Stang, E.3
Larsen, A.M.4
Johannessen, L.E.5
Madshus, I.H.6
-
41
-
-
0037178754
-
Modulation of postendocytic sorting of G protein-coupled receptors
-
Most G-protein-coupled receptors require β-arrestin to be endocytosed. This report identifies a G-protein-coupled receptor-associated sorting protein (GASP) that seems to be required for lysosomal sorting of these receptors after endocytosis.
-
Whistler J.L., Enquist J., Marley A., Fong J., Gladher F., Tsuruda P., Murray S.R., Von Zastrow M. Modulation of postendocytic sorting of G protein-coupled receptors. Science. 297:2002;615-620 Most G-protein-coupled receptors require β-arrestin to be endocytosed. This report identifies a G-protein-coupled receptor-associated sorting protein (GASP) that seems to be required for lysosomal sorting of these receptors after endocytosis.
-
(2002)
Science
, vol.297
, pp. 615-620
-
-
Whistler, J.L.1
Enquist, J.2
Marley, A.3
Fong, J.4
Gladher, F.5
Tsuruda, P.6
Murray, S.R.7
Von Zastrow, M.8
-
42
-
-
0037200109
-
Separation and characterization of late endosomal membrane domains
-
Late multivesicular endosomes have been subject to suborganellar fractionation in the absence of detergent. This provides new insights into how late endosomal proteins and especially lipids are distributed within these compartments. The data indicate that there are at least two populations of internal vesicles, which contain the phospholipids phosphatidylcholine or lyso-bisphosphatidic acid, respectively.
-
Kobayashi T., Beuchat M.H., Chevallier J., Makino A., Mayran N., Escola J.M., Lebrand C., Cosson P., Kobayashi T., Gruenberg J. Separation and characterization of late endosomal membrane domains. J. Biol. Chem. 277:2002;32157-32164 Late multivesicular endosomes have been subject to suborganellar fractionation in the absence of detergent. This provides new insights into how late endosomal proteins and especially lipids are distributed within these compartments. The data indicate that there are at least two populations of internal vesicles, which contain the phospholipids phosphatidylcholine or lyso-bisphosphatidic acid, respectively.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 32157-32164
-
-
Kobayashi, T.1
Beuchat, M.H.2
Chevallier, J.3
Makino, A.4
Mayran, N.5
Escola, J.M.6
Lebrand, C.7
Cosson, P.8
Kobayashi, T.9
Gruenberg, J.10
-
43
-
-
0035871081
-
Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins
-
Gillooly D.J., Simonsen A., Stenmark H. Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins. Biochem. J. 355:2001;249-258.
-
(2001)
Biochem. J.
, vol.355
, pp. 249-258
-
-
Gillooly, D.J.1
Simonsen, A.2
Stenmark, H.3
-
44
-
-
0035945343
-
Human VPS34 is required for internal vesicle formation within multivesicular bodies
-
Futter C.E., Collinson L.M., Backer J.M., Hopkins C.R. Human VPS34 is required for internal vesicle formation within multivesicular bodies. J. Cell Biol. 155:2001;1251-1263.
-
(2001)
J. Cell Biol.
, vol.155
, pp. 1251-1263
-
-
Futter, C.E.1
Collinson, L.M.2
Backer, J.M.3
Hopkins, C.R.4
-
45
-
-
0034282751
-
Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
-
Gillooly D.J., Morrow I.C., Lindsay M., Gould R., Bryant N.J., Gaullier J.-M., Parton R.G., Stenmark H. Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J. 19:2000;4577-4588.
-
(2000)
EMBO J.
, vol.19
, pp. 4577-4588
-
-
Gillooly, D.J.1
Morrow, I.C.2
Lindsay, M.3
Gould, R.4
Bryant, N.J.5
Gaullier, J.-M.6
Parton, R.G.7
Stenmark, H.8
-
47
-
-
0034941051
-
FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes
-
Raiborg C., Bremnes B., Mehlum A., Gillooly D.J., Stang E., Stenmark H. FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes. J. Cell Sci. 114:2001;2255-2263.
-
(2001)
J. Cell Sci.
, vol.114
, pp. 2255-2263
-
-
Raiborg, C.1
Bremnes, B.2
Mehlum, A.3
Gillooly, D.J.4
Stang, E.5
Stenmark, H.6
-
48
-
-
0030949124
-
Functional rafts in cell membranes
-
Simons K., Ikonen E. Functional rafts in cell membranes. Nature. 387:1997;569-572.
-
(1997)
Nature
, vol.387
, pp. 569-572
-
-
Simons, K.1
Ikonen, E.2
-
49
-
-
0032510559
-
A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
-
Kobayashi T., Stang E., Fang K.S., De Moerloose P., Parton R.G., Gruenberg J. A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature. 392:1998;193-197.
-
(1998)
Nature
, vol.392
, pp. 193-197
-
-
Kobayashi, T.1
Stang, E.2
Fang, K.S.3
De Moerloose, P.4
Parton, R.G.5
Gruenberg, J.6
-
51
-
-
0036697166
-
Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular bodies
-
The class E Vps proteins Vps22, Vps25 and Vps36 are shown to assemble into a 155 kDa protein complex, ESCRT-II. It acts downstream of the previously described ESCRT-I complex [24] and is transiently associated with endosomal membranes. Immunoprecipitation experiments indicate that components of ESCRT-II can interact with components of ESCRT-III, and subunits of ESCRT-III become more cytosolic in cells that lack ESCRT-II components. The authors suggest that ESCRT-II can initiate the formation of ESCRT-III on endosomal membranes.
-
Babst M., Katzmann D.J., Snyder W.B., Wendland B., Emr S.D. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular bodies. Dev. Cell. 3:2002;283-289 The class E Vps proteins Vps22, Vps25 and Vps36 are shown to assemble into a 155 kDa protein complex, ESCRT-II. It acts downstream of the previously described ESCRT-I complex [24] and is transiently associated with endosomal membranes. Immunoprecipitation experiments indicate that components of ESCRT-II can interact with components of ESCRT-III, and subunits of ESCRT-III become more cytosolic in cells that lack ESCRT-II components. The authors suggest that ESCRT-II can initiate the formation of ESCRT-III on endosomal membranes.
-
(2002)
Dev. Cell
, vol.3
, pp. 283-289
-
-
Babst, M.1
Katzmann, D.J.2
Snyder, W.B.3
Wendland, B.4
Emr, S.D.5
-
52
-
-
0036845476
-
Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Np14
-
Meyer H.H., Wang Y., Warren G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Np14. EMBO J. 21:2002;5645-5652.
-
(2002)
EMBO J.
, vol.21
, pp. 5645-5652
-
-
Meyer, H.H.1
Wang, Y.2
Warren, G.3
-
54
-
-
0036900880
-
Mechanisms of enveloped RNA virus budding
-
Virus budding and multivesicular endosome formation are two topologically similar events. Recent studies have identified a molecular link between these processes, as discussed in this article.
-
Pornillos O., Garrus J.E., Sundquist W.I. Mechanisms of enveloped RNA virus budding. Trends Cell Biol. 12:2002;569-579 Virus budding and multivesicular endosome formation are two topologically similar events. Recent studies have identified a molecular link between these processes, as discussed in this article.
-
(2002)
Trends Cell Biol.
, vol.12
, pp. 569-579
-
-
Pornillos, O.1
Garrus, J.E.2
Sundquist, W.I.3
-
55
-
-
17944363138
-
Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
-
Garrus J.E., von Schwedler U.K., Pornillos O.W., Morham S.G., Zavitz K.H., Wang H.E., Wettstein D.A., Stray K.M., Cote M., Rich R.L.et al. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell. 107:2001;55-65.
-
(2001)
Cell
, vol.107
, pp. 55-65
-
-
Garrus, J.E.1
Von Schwedler, U.K.2
Pornillos, O.W.3
Morham, S.G.4
Zavitz, K.H.5
Wang, H.E.6
Wettstein, D.A.7
Stray, K.M.8
Cote, M.9
Rich, R.L.10
-
56
-
-
0036829172
-
Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
-
•]), the authors continue their investigation of the structure of this domain in complex with the HIV late-domain PTAP sequence. Interestingly, a similar motif (PSAP) is found in Hrs.
-
•]), the authors continue their investigation of the structure of this domain in complex with the HIV late-domain PTAP sequence. Interestingly, a similar motif (PSAP) is found in Hrs.
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 812-817
-
-
Pornillos, O.1
Alam, S.L.2
Davis, D.R.3
Sundquist, W.I.4
-
57
-
-
0036788110
-
Human macrophages accumulate HIV-1 particles in MHC II compartments
-
By studying HIV-infected macrophages using electron microscopy, the authors show that virus particles accumulate in multivesicular compartments which are enriched in MHC class II and CD63. The data suggest that virus might access the lumen of this compartment by budding from the limiting membrane, similar to the formation of internal vesicles in multivesicular endosomes.
-
Raposo G., Moore M., Innes D., Leijendekker R., Leigh-Brown A., Benaroch P., Geuze H. Human macrophages accumulate HIV-1 particles in MHC II compartments. Traffic. 3:2002;718-729 By studying HIV-infected macrophages using electron microscopy, the authors show that virus particles accumulate in multivesicular compartments which are enriched in MHC class II and CD63. The data suggest that virus might access the lumen of this compartment by budding from the limiting membrane, similar to the formation of internal vesicles in multivesicular endosomes.
-
(2002)
Traffic
, vol.3
, pp. 718-729
-
-
Raposo, G.1
Moore, M.2
Innes, D.3
Leijendekker, R.4
Leigh-Brown, A.5
Benaroch, P.6
Geuze, H.7
-
58
-
-
0037436346
-
Ebola virus matrix protein vp40 interaction with human cellular factors Tsg101 and Nedd4
-
This report shows that the V40 protein from Ebola virus can interact with human Nedd4 and Tsg101 in vitro. The WW domain 3 of Nedd4 is necessary and sufficient for binding to the PPXY motif of V40, whereas the UEV domain of Tsg101 is sufficient to bind the PTAP domain of the virus protein.
-
Timmins J., Schoehn G., Ricard-Blum S., Scianimanico S., Vernet T., Ruigrok R.W., Weissenhorn W. Ebola virus matrix protein vp40 interaction with human cellular factors Tsg101 and Nedd4. J. Mol. Biol. 326:2003;493-502 This report shows that the V40 protein from Ebola virus can interact with human Nedd4 and Tsg101 in vitro. The WW domain 3 of Nedd4 is necessary and sufficient for binding to the PPXY motif of V40, whereas the UEV domain of Tsg101 is sufficient to bind the PTAP domain of the virus protein.
-
(2003)
J. Mol. Biol.
, vol.326
, pp. 493-502
-
-
Timmins, J.1
Schoehn, G.2
Ricard-Blum, S.3
Scianimanico, S.4
Vernet, T.5
Ruigrok, R.W.6
Weissenhorn, W.7
-
59
-
-
0037303193
-
Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4
-
Mutational analysis of the PTAPPEY sequence indicates that the PTAP and PPEY motifs can function separately in virus budding, and the PTAP motif recruits Tsg101 into the virus buds. Furthermore, a dominant-negative mutant of Vps4 inhibits the budding of the Ebola virus.
-
Licata J.M., Simpson-Holley M., Wright N.T., Han Z., Paragas J., Harty R.N. Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4. J. Virol. 77:2003;1812-1819 Mutational analysis of the PTAPPEY sequence indicates that the PTAP and PPEY motifs can function separately in virus budding, and the PTAP motif recruits Tsg101 into the virus buds. Furthermore, a dominant-negative mutant of Vps4 inhibits the budding of the Ebola virus.
-
(2003)
J. Virol.
, vol.77
, pp. 1812-1819
-
-
Licata, J.M.1
Simpson-Holley, M.2
Wright, N.T.3
Han, Z.4
Paragas, J.5
Harty, R.N.6
-
60
-
-
0037093467
-
Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation
-
K3 is the first example of a viral gene product that can subvert the trafficking of a host protein via the ubiquitin-dependent multivesicular endosome sorting machinery.
-
Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G., Lehner P.J. Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation. EMBO J. 21:2002;2418-2429 K3 is the first example of a viral gene product that can subvert the trafficking of a host protein via the ubiquitin-dependent multivesicular endosome sorting machinery.
-
(2002)
EMBO J.
, vol.21
, pp. 2418-2429
-
-
Hewitt, E.W.1
Duncan, L.2
Mufti, D.3
Baker, J.4
Stevenson, P.G.5
Lehner, P.J.6
-
61
-
-
0037228216
-
The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4
-
This study gives another intriguing example of how viruses can induce endocytic downregulation of host proteins, thereby evading the cellular immune response.
-
Mansouri M., Bartee E., Gouveia K., Hovey Nerenberg B.T., Barrett J., Thomas L., Thomas G., McFadden G., Fruh K. The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4. J. Virol. 77:2003;1427-1440 This study gives another intriguing example of how viruses can induce endocytic downregulation of host proteins, thereby evading the cellular immune response.
-
(2003)
J. Virol.
, vol.77
, pp. 1427-1440
-
-
Mansouri, M.1
Bartee, E.2
Gouveia, K.3
Hovey Nerenberg, B.T.4
Barrett, J.5
Thomas, L.6
Thomas, G.7
McFadden, G.8
Fruh, K.9
-
62
-
-
0036099724
-
Ubiquitin-independent entry into the yeast recycling pathway
-
In this report, trafficking of the yeast a-factor receptor Ste3p is investigated. While the constitutive ligand-independent uptake and vacuolar degradation of the receptor are dependent on receptor ubiquitination, ligand-dependent internalisation and recycling are not.
-
Chen L., Davis N.G. Ubiquitin-independent entry into the yeast recycling pathway. Traffic. 3:2002;110-123 In this report, trafficking of the yeast a-factor receptor Ste3p is investigated. While the constitutive ligand-independent uptake and vacuolar degradation of the receptor are dependent on receptor ubiquitination, ligand-dependent internalisation and recycling are not.
-
(2002)
Traffic
, vol.3
, pp. 110-123
-
-
Chen, L.1
Davis, N.G.2
-
63
-
-
0038394715
-
Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
-
•] show evidence that receptors for epidermal growth factor and platelet-derived growth factor become multiply monoubiquitinated (and not polyubiquitinated) upon ligand binding. A single attached ubiquitin appears to be sufficient for endocytosis and lysosomal degradation.
-
•] show evidence that receptors for epidermal growth factor and platelet-derived growth factor become multiply monoubiquitinated (and not polyubiquitinated) upon ligand binding. A single attached ubiquitin appears to be sufficient for endocytosis and lysosomal degradation.
-
(2003)
Nature Cell Biol.
, vol.5
, pp. 461-466
-
-
Haglund, K.1
Sigismund, S.2
Polo, S.3
Szymkiewicz, I.4
Di Fiore, P.P.5
Dikic, I.6
-
64
-
-
0037677208
-
Endocytosis of receptor tyrosine kinases is driven by mono-, not poly-, ubiquitylation
-
published online 28 April 2003. DOI 10.1074/jbc.C300096200.
-
Mosesson Y, Shtiegman K, Katz M, Zwang Y, Vereb G, Szollosi J, Yarden Y: Endocytosis of receptor tyrosine kinases is driven by mono-, not poly-, ubiquitylation. J Biol Chem 2003, published online 28 April 2003. DOI 10.1074/jbc.C300096200.
-
(2003)
J Biol Chem
-
-
Mosesson, Y.1
Shtiegman, K.2
Katz, M.3
Zwang, Y.4
Vereb, G.5
Szollosi, J.6
Yarden, Y.7
-
65
-
-
0037695000
-
Endosomal dynamics of met determine signaling output
-
The proteasomal inhibitor lactacystin alters the routing of the endocytosed hepatocyte growth factor receptor (Met). Lactacystin causes the endocytosed receptor to recycle to the plasma membrane instead of being degraded in lysosomes, and phosphorylation of the receptor is prevented. Reduction of cellular Hrs levels retards degradation and dephosphorylation of Met.
-
Hammond D.E., Carter S., McCullough J., Urbe S., Vande W.G., Clague M.J. Endosomal dynamics of met determine signaling output. Mol. Biol. Cell. 14:2003;1346-1354 The proteasomal inhibitor lactacystin alters the routing of the endocytosed hepatocyte growth factor receptor (Met). Lactacystin causes the endocytosed receptor to recycle to the plasma membrane instead of being degraded in lysosomes, and phosphorylation of the receptor is prevented. Reduction of cellular Hrs levels retards degradation and dephosphorylation of Met.
-
(2003)
Mol. Biol. Cell
, vol.14
, pp. 1346-1354
-
-
Hammond, D.E.1
Carter, S.2
McCullough, J.3
Urbe, S.4
Vande, W.G.5
Clague, M.J.6
-
66
-
-
0345381737
-
The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor
-
Vecchione A., Marchese A., Henry P., Rotin D., Morrione A. The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor. Mol. Cell Biol. 23:2003;3363-3372.
-
(2003)
Mol. Cell Biol.
, vol.23
, pp. 3363-3372
-
-
Vecchione, A.1
Marchese, A.2
Henry, P.3
Rotin, D.4
Morrione, A.5
-
67
-
-
0345616428
-
A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
-
Shih S.C., Prag G., Francis S.A., Sutanto M.A., Hurley J.H., Hicke L. A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain. EMBO J. 22:2003;1273-1281.
-
(2003)
EMBO J.
, vol.22
, pp. 1273-1281
-
-
Shih, S.C.1
Prag, G.2
Francis, S.A.3
Sutanto, M.A.4
Hurley, J.H.5
Hicke, L.6
-
68
-
-
0037316409
-
Ubiquitin signals protein trafficking via interaction with a novel ubiquitin binding domain in the membrane fusion regulator, Vps9p
-
Donaldson K.M., Yin H., Gekakis N., Supek F., Joazeiro C.A. Ubiquitin signals protein trafficking via interaction with a novel ubiquitin binding domain in the membrane fusion regulator, Vps9p. Curr. Biol. 13:2003;258-262.
-
(2003)
Curr. Biol.
, vol.13
, pp. 258-262
-
-
Donaldson, K.M.1
Yin, H.2
Gekakis, N.3
Supek, F.4
Joazeiro, C.A.5
|