메뉴 건너뛰기




Volumn 75, Issue 1, 2000, Pages 48-55

Ubiquitination and degradation of the zebrafish paired-like homeobox protein Vsx-1

Author keywords

26S proteasome; Bipolar cells; Chx10; Retina; Ubiquitin

Indexed keywords

HOMEODOMAIN PROTEIN; PROTEASOME;

EID: 0034089125     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0750048.x     Document Type: Article
Times cited : (12)

References (42)
  • 1
    • 0031681282 scopus 로고    scopus 로고
    • Degradation of myogenic transcription factor MyoD by the ubiquitin pathway in vivo and in vitro: Regulation by specific DNA binding
    • Abu Hatoum O., Gross-Mesilaty S., Breitschopf K., Hoffman A., Gonen H., Ciechanover A., and Bengal E. (1998) Degradation of myogenic transcription factor MyoD by the ubiquitin pathway in vivo and in vitro: regulation by specific DNA binding. Mol. Cell. Biol. 18, 5670-5677.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5670-5677
    • Abu Hatoum, O.1    Gross-Mesilaty, S.2    Breitschopf, K.3    Hoffman, A.4    Gonen, H.5    Ciechanover, A.6    Bengal, E.7
  • 2
    • 0030993618 scopus 로고    scopus 로고
    • Inactivation of the zebrafish homologue of Chx10 by antisense oligonucleotides causes eye malformations similar to the ocular retardation phenotype
    • Barabino S. M., Spada F., Cotelli F., and Boncinelli E. (1997) Inactivation of the zebrafish homologue of Chx10 by antisense oligonucleotides causes eye malformations similar to the ocular retardation phenotype. Mech. Dev. 63, 133-143.
    • (1997) Mech. Dev. , vol.63 , pp. 133-143
    • Barabino, S.M.1    Spada, F.2    Cotelli, F.3    Boncinelli, E.4
  • 3
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-kappa B
    • Beg A. A., Sha W. C., Bronson R. T., Ghosh S., and Baltimore D. (1995) Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-kappa B. Nature 376, 167-170.
    • (1995) Nature , vol.376 , pp. 167-170
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Ghosh, S.4    Baltimore, D.5
  • 4
    • 0030003157 scopus 로고    scopus 로고
    • Requirements for dE2F function in proliferating cells and in post-mitotic differentiating cells
    • Brook A., Xie J. E., Du W., and Dyson N. (1996) Requirements for dE2F function in proliferating cells and in post-mitotic differentiating cells. EMBO J. 15, 3676-3683.
    • (1996) EMBO J. , vol.15 , pp. 3676-3683
    • Brook, A.1    Xie, J.E.2    Du, W.3    Dyson, N.4
  • 6
    • 0030903750 scopus 로고    scopus 로고
    • Regulation of E2F through ubiquitin-proteasome-dependent degradation: Stabilization by the pRB tumor suppressor protein
    • Campanero M. R. and Flemington E. K. (1997) Regulation of E2F through ubiquitin-proteasome-dependent degradation: stabilization by the pRB tumor suppressor protein. Proc. Natl. Acad. Sci. USA 94, 2221-2226.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2221-2226
    • Campanero, M.R.1    Flemington, E.K.2
  • 7
  • 9
    • 0029957947 scopus 로고    scopus 로고
    • Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation
    • Clurman B. E., Sheaff R. J., Thress K., Groudine M., and Roberts J. M. (1996) Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation. Genes Dev. 10, 1979-1990.
    • (1996) Genes Dev. , vol.10 , pp. 1979-1990
    • Clurman, B.E.1    Sheaff, R.J.2    Thress, K.3    Groudine, M.4    Roberts, J.M.5
  • 10
    • 0030999057 scopus 로고    scopus 로고
    • NF-kappa B RelA-deficient lymphocytes: Normal development of T cells and B cells, impaired production of IgA and IgG1 and reduced proliferative responses
    • Doi T. S., Takahashi T., Taguchi O., Azuma T., and Obata Y. (1997) NF-kappa B RelA-deficient lymphocytes: normal development of T cells and B cells, impaired production of IgA and IgG1 and reduced proliferative responses. J. Exp. Med. 185, 953-961.
    • (1997) J. Exp. Med. , vol.185 , pp. 953-961
    • Doi, T.S.1    Takahashi, T.2    Taguchi, O.3    Azuma, T.4    Obata, Y.5
  • 12
    • 0029790558 scopus 로고    scopus 로고
    • Transcription factor genes and the developing eye: A genetic perspective
    • Freund C., Horsford D. and McInnes R. (1996) Transcription factor genes and the developing eye: a genetic perspective. Hum. Mol. Genet. 5, 1471-1488.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1471-1488
    • Freund, C.1    Horsford, D.2    McInnes, R.3
  • 13
    • 0030979167 scopus 로고    scopus 로고
    • rax, a novel paired-type homeobox gene, shows expression in the anterior neural fold and developing retina
    • Furukawa T., Kozak C. A., and Cepko C. L. (1997) rax, a novel paired-type homeobox gene, shows expression in the anterior neural fold and developing retina. Proc. Natl. Acad. Sci. USA 94, 3088-3093.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3088-3093
    • Furukawa, T.1    Kozak, C.A.2    Cepko, C.L.3
  • 14
    • 0029797841 scopus 로고    scopus 로고
    • Degradation of E2F by the ubiquitin-proteasome pathway: Regulation by retinoblastoma family proteins and adenovirus transforming proteins
    • Hateboer G., Kerkhoven R. M., Shvarts A., Bernards R., and Beijersbergen R. L. (1996) Degradation of E2F by the ubiquitin-proteasome pathway: regulation by retinoblastoma family proteins and adenovirus transforming proteins. Genes Dev. 10, 2960-2970.
    • (1996) Genes Dev. , vol.10 , pp. 2960-2970
    • Hateboer, G.1    Kerkhoven, R.M.2    Shvarts, A.3    Bernards, R.4    Beijersbergen, R.L.5
  • 15
    • 0031886093 scopus 로고    scopus 로고
    • Regulation of cell proliferation by the E2F transcription factors
    • Helin K. (1998) Regulation of cell proliferation by the E2F transcription factors. Curr. Opin. Genet. Dev. 8, 28-35.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 28-35
    • Helin, K.1
  • 16
    • 0023768491 scopus 로고
    • Ubiquitin-mediated protein degradation
    • Hershko A. (1988) Ubiquitin-mediated protein degradation. J. Biol. Chem. 263, 15237-15240.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15237-15240
    • Hershko, A.1
  • 17
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. (1996) Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 18
    • 0025853324 scopus 로고
    • The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo
    • Hochstrasser M., Ellison M. J., Chau V., and Varshavsky A. (1991) The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo. Proc. Natl. Acad. Sci. USA 88, 4606-4610.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4606-4610
    • Hochstrasser, M.1    Ellison, M.J.2    Chau, V.3    Varshavsky, A.4
  • 19
    • 0031434589 scopus 로고    scopus 로고
    • The deubiquitination enzyme fat facets negatively regulates RTK/Ras/MAPK signalling during Drosophila eye development
    • Isaksson A., Peverali F. A., Kockel L., Mlodzik M., and Bohmann D. (1997) The deubiquitination enzyme fat facets negatively regulates RTK/Ras/MAPK signalling during Drosophila eye development. Mech. Dev. 68, 59-67.
    • (1997) Mech. Dev. , vol.68 , pp. 59-67
    • Isaksson, A.1    Peverali, F.A.2    Kockel, L.3    Mlodzik, M.4    Bohmann, D.5
  • 20
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome
    • Jariel-Encontre I., Pariat M., Martin F., Carillo S., Salvat C., and Piechaczyk M. (1995) Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome. J. Biol Chem. 270, 11623-11627.
    • (1995) J. Biol Chem. , vol.270 , pp. 11623-11627
    • Jariel-Encontre, I.1    Pariat, M.2    Martin, F.3    Carillo, S.4    Salvat, C.5    Piechaczyk, M.6
  • 21
    • 0032563319 scopus 로고    scopus 로고
    • Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway
    • Johnson P. R., Swanson R., Rakhilina L., and Hochstrasser M. (1998) Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway. Cell 94, 217-227.
    • (1998) Cell , vol.94 , pp. 217-227
    • Johnson, P.R.1    Swanson, R.2    Rakhilina, L.3    Hochstrasser, M.4
  • 22
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M., Hoppe T., Schlenker S., Ulrich H. D., Mayer T. U., and Jentsch S. (1999) A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 23
    • 0028607143 scopus 로고
    • Regulated degradation of the transcription factor Gen4
    • Kornitzer D., Raboy B., Kulka R. G., and Fink G. R. (1994) Regulated degradation of the transcription factor Gen4. EMBO J. 13, 6021-6030.
    • (1994) EMBO J. , vol.13 , pp. 6021-6030
    • Kornitzer, D.1    Raboy, B.2    Kulka, R.G.3    Fink, G.R.4
  • 24
    • 0027968803 scopus 로고
    • Restricted expression of a new paired-class homeobox gene in normal and regenerating adult goldfish retina
    • Levine E. M., Hitchcock P. F., Glasgow E., and Schechter N. (1994) Restricted expression of a new paired-class homeobox gene in normal and regenerating adult goldfish retina. J. Comp. Neurol. 348, 596-606.
    • (1994) J. Comp. Neurol. , vol.348 , pp. 596-606
    • Levine, E.M.1    Hitchcock, P.F.2    Glasgow, E.3    Schechter, N.4
  • 25
    • 0030884705 scopus 로고    scopus 로고
    • Vsx-1 and Vsx-2: Two Chx10-like homeobox genes expressed in overlapping domains in the adult goldfish retina
    • Levine E. M., Passini M., Hitchcock P. F., Glasgow E., and Schechter N. (1997) Vsx-1 and Vsx-2: two Chx10-like homeobox genes expressed in overlapping domains in the adult goldfish retina. J. Comp. Neurol. 387, 439-448.
    • (1997) J. Comp. Neurol. , vol.387 , pp. 439-448
    • Levine, E.M.1    Passini, M.2    Hitchcock, P.F.3    Glasgow, E.4    Schechter, N.5
  • 26
    • 0031961993 scopus 로고    scopus 로고
    • A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease
    • Marchai C., Haguenauer-Tsapis R., and Urban-Grimal D. (1998) A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease. Mol. Cell. Biol. 18, 314-321.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 314-321
    • Marchai, C.1    Haguenauer-Tsapis, R.2    Urban-Grimal, D.3
  • 27
    • 0031001710 scopus 로고    scopus 로고
    • The Rx homeobox gene is essential for vertebrate eye development
    • Mathers P. H., Grinberg A., Mahon K. A., and Jamrich M. (1997) The Rx homeobox gene is essential for vertebrate eye development. Nature 387, 603-607.
    • (1997) Nature , vol.387 , pp. 603-607
    • Mathers, P.H.1    Grinberg, A.2    Mahon, K.A.3    Jamrich, M.4
  • 28
    • 0030980493 scopus 로고    scopus 로고
    • Preproparathyroid hormone-related protein, a secreted peptide, is a substrate for the ubiquitin proteolytic system
    • Meerovitch K., Wing S., and Goltzman D. (1997) Preproparathyroid hormone-related protein, a secreted peptide, is a substrate for the ubiquitin proteolytic system. J. Biol. Chem. 272, 6706-6713.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6706-6713
    • Meerovitch, K.1    Wing, S.2    Goltzman, D.3
  • 29
    • 0027185303 scopus 로고
    • The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes
    • Muralidhar M. G. and Thomas J. B. (1993) The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes. Neuron 11, 253-266.
    • (1993) Neuron , vol.11 , pp. 253-266
    • Muralidhar, M.G.1    Thomas, J.B.2
  • 30
    • 0028271574 scopus 로고
    • bendless, a Drosophila gene affecting neuronal connectivity, encodes a ubiquitin-conjugating enzyme homolog
    • Oh C. E., McMahon R., Benzer S., and Tanouye M. A. (1994) bendless, a Drosophila gene affecting neuronal connectivity, encodes a ubiquitin-conjugating enzyme homolog. J. Neurosci. 14, 3166-3179.
    • (1994) J. Neurosci. , vol.14 , pp. 3166-3179
    • Oh, C.E.1    McMahon, R.2    Benzer, S.3    Tanouye, M.A.4
  • 31
    • 0030724047 scopus 로고    scopus 로고
    • Vsx-1 and Vsx-2: Differential expression of two paired-like homeobox genes during zebrafish and goldfish retinogenesis
    • Passini M. A., Levine E. M., Canger A. K., Raymond P. A., and Schechter N. (1997) Vsx-1 and Vsx-2: differential expression of two paired-like homeobox genes during zebrafish and goldfish retinogenesis. J. Comp. Neurol. 388, 495-505.
    • (1997) J. Comp. Neurol. , vol.388 , pp. 495-505
    • Passini, M.A.1    Levine, E.M.2    Canger, A.K.3    Raymond, P.A.4    Schechter, N.5
  • 33
    • 17344375394 scopus 로고    scopus 로고
    • vsx2, a gene encoding a paired-type homeodomain, is expressed in the retina hindbrain, and spinal cord during goldfish embryogenesis
    • Passini M. A., Raymond P. A., and Schechter N. (1998b) vsx2, a gene encoding a paired-type homeodomain, is expressed in the retina hindbrain, and spinal cord during goldfish embryogenesis. Brain Res. Dev. Brain Res. 109, 129-135.
    • (1998) Brain Res. Dev. Brain Res. , vol.109 , pp. 129-135
    • Passini, M.A.1    Raymond, P.A.2    Schechter, N.3
  • 35
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • Salceda S. and Caro J. (1997) Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J. Biol. Chem. 272, 22642-22647.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 36
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize Myc
    • Salghetti S. E., Kim S. Y., and Tansey W. P. (1999) Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc. EMBO J. 18, 717-726.
    • (1999) EMBO J. , vol.18 , pp. 717-726
    • Salghetti, S.E.1    Kim, S.Y.2    Tansey, W.P.3
  • 37
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner M., Werness B. A., Huibregtse J. M., Levine A. J., and Howley P. M. (1990) The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63, 1129-1136.
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 38
    • 0021931262 scopus 로고
    • An immunoblot study of neurofilament degradation in situ and during calcium-activated proteolysis
    • Schlaepfer W. W., Lee C., Lee V. M.-Y., and Zimmerman U.-J. (1985) An immunoblot study of neurofilament degradation in situ and during calcium-activated proteolysis. J. Neurochem. 44, 502-509.
    • (1985) J. Neurochem. , vol.44 , pp. 502-509
    • Schlaepfer, W.W.1    Lee, C.2    Lee, V.M.-Y.3    Zimmerman, U.-J.4
  • 39
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier M., Staszewski L. M., and Bohmann D. (1994) Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78, 787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 40
    • 0022607144 scopus 로고
    • 2+-activated neutral thiol proteinase from Ehrlich ascites tumor cells and porcine kidney
    • 2+-activated neutral thiol proteinase from Ehrlich ascites tumor cells and porcine kidney. Biosci. Rep. 6, 57-64.
    • (1986) Biosci. Rep. , vol.6 , pp. 57-64
    • Vorgias, C.E.1    Traub, P.2
  • 41
    • 0029737650 scopus 로고    scopus 로고
    • Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E
    • Won K. A. and Reed S. I. (1996) Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J. 15, 4182-4193.
    • (1996) EMBO J. , vol.15 , pp. 4182-4193
    • Won, K.A.1    Reed, S.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.