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Volumn 287, Issue 9, 2012, Pages 6503-6517

Cytosolic carboxypeptidase 1 is involved in processing α- and β-tubulin

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE; CYTOSOLIC; HUMAN EMBRYONIC KIDNEYS; IN-VITRO; KNOCK OUTS; MICROTUBULES; MOUSE BRAIN; OVER-EXPRESSION; PRIMARY FUNCTIONS; PURKINJE CELLS; SIDE-CHAINS;

EID: 84857499438     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.309138     Document Type: Article
Times cited : (70)

References (54)
  • 1
    • 0034533467 scopus 로고    scopus 로고
    • Regenerating motor neurons express Nna1, a novel ATP/GTP-binding protein related to zinc carboxypeptidases
    • DOI 10.1006/mcne.2000.0900
    • Harris, A., Morgan, J. I., Pecot, M., Soumare, A., Osborne, A., and Soares, H. D. (2000) Regenerating motor neurons express Nna1, a novel ATP/GTP-binding protein related to zinc carboxypeptidases. Mol. Cell. Neurosci. 16, 578-596 (Pubitemid 32001307)
    • (2000) Molecular and Cellular Neuroscience , vol.16 , Issue.5 , pp. 578-596
    • Harris, A.1    Morgan, J.I.2    Pecot, M.3    Soumare, A.4    Osborne, A.5    Soares, H.D.6
  • 4
    • 0037040583 scopus 로고    scopus 로고
    • Purkinje cell degeneration (pcd) phenotypes caused by mutations in the axotomy-induced gene, Nna1
    • DOI 10.1126/science.1068912
    • Fernandez-Gonzalez, A., La Spada, A. R., Treadaway, J., Higdon, J. C., Harris, B. S., Sidman, R. L., Morgan, J. I., and Zuo, J. (2002) Purkinje cell degeneration (pcd) phenotypes caused by mutations in the axotomy-induced gene, Nna1. Science 295, 1904-1906 (Pubitemid 34214129)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1904-1906
    • Fernandez-Gonzalez, A.1    La, S.A.R.2    Treadaway, J.3    Higdon, J.C.4    Harris, B.S.5    Sidman, R.L.6    Morgan, J.I.7    Zuo, J.8
  • 5
    • 2042422363 scopus 로고
    • Purkinje cell degeneration, a new neurological mutation in the mouse
    • Mullen, R. J., Eicher, E. M., and Sidman, R. L. (1976) Purkinje cell degeneration, a new neurological mutation in the mouse. Proc. Natl. Acad. Sci. U.S.A. 73, 208-212
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 208-212
    • Mullen, R.J.1    Eicher, E.M.2    Sidman, R.L.3
  • 6
    • 33847661633 scopus 로고    scopus 로고
    • The Purkinje cell degeneration (pcd) mouse: An unexpected molecular link between neuronal degeneration and regeneration
    • DOI 10.1016/j.brainres.2006.07.065, PII S0006899306022037, A Catalog of the Neurological Mutants of the Mouse Revisited
    • Wang, T., and Morgan, J. I. (2007) The Purkinje cell degeneration (pcd) mouse. An unexpected molecular link between neuronal degeneration and regeneration. Brain Res. 1140, 26-40 (Pubitemid 46356298)
    • (2007) Brain Research , vol.1140 , Issue.1 , pp. 26-40
    • Wang, T.1    Morgan, J.I.2
  • 7
    • 33748804989 scopus 로고    scopus 로고
    • The carboxypeptidase-like substrate-binding site in Nna1 is essential for the rescue of the Purkinje cell degeneration (pcd) phenotype
    • DOI 10.1016/j.mcn.2006.07.009, PII S1044743106001631
    • Wang, T., Parris, J., Li, L., and Morgan, J. I. (2006) The carboxypeptidase-like substrate-binding site in Nna1 is essential for the rescue of the Purkinje cell degeneration (pcd) phenotype. Mol. Cell. Neurosci. 33, 200-213 (Pubitemid 44415492)
    • (2006) Molecular and Cellular Neuroscience , vol.33 , Issue.2 , pp. 200-213
    • Wang, T.1    Parris, J.2    Li, L.3    Morgan, J.I.4
  • 8
    • 48749085672 scopus 로고    scopus 로고
    • The zinc-binding domain of Nna1 is required to prevent retinal photoreceptor loss and cerebellar ataxia in Purkinje cell degeneration (pcd) mice
    • Chakrabarti, L., Eng, J., Martinez, R. A., Jackson, S., Huang, J., Possin, D. E., Sopher, B. L., and La Spada, A. R. (2008) The zinc-binding domain of Nna1 is required to prevent retinal photoreceptor loss and cerebellar ataxia in Purkinje cell degeneration (pcd) mice. Vision Res. 48, 1999-2005
    • (2008) Vision Res. , vol.48 , pp. 1999-2005
    • Chakrabarti, L.1    Eng, J.2    Martinez, R.A.3    Jackson, S.4    Huang, J.5    Possin, D.E.6    Sopher, B.L.7    La Spada, A.R.8
  • 9
    • 0017927928 scopus 로고
    • The development and degeneration of Purkinje cells in pcd mutant mice
    • Landis, S. C., and Mullen, R. J. (1978) The development and degeneration of Purkinje cells in pcd mutant mice. J. Comp. Neurol. 177, 125-143 (Pubitemid 8241768)
    • (1978) Journal of Comparative Neurology , vol.177 , Issue.1 , pp. 125-143
    • Landis, S.C.1    Mullen, R.J.2
  • 10
    • 33750619522 scopus 로고    scopus 로고
    • Pre-neurodegeneration of mitral cells in the pcd mutant mouse is associated with DNA damage, transcriptional repression, and reorganization of nuclear speckles and Cajal bodies
    • DOI 10.1016/j.mcn.2006.08.002, PII S1044743106001709
    • Valero, J., Berciano, M. T., Weruaga, E., Lafarga, M., and Alonso, J. R. (2006) Pre-neurodegeneration of mitral cells in the pcd mutant mouse is associated with DNA damage, transcriptional repression, and reorganization of nuclear speckles and Cajal bodies. Mol. Cell. Neurosci. 33, 283-295 (Pubitemid 44692493)
    • (2006) Molecular and Cellular Neuroscience , vol.33 , Issue.3 , pp. 283-295
    • Valero, J.1    Berciano, M.T.2    Weruaga, E.3    Lafarga, M.4    Alonso, J.R.5
  • 11
    • 80051516014 scopus 로고    scopus 로고
    • Purkinje cell degeneration in pcd mice reveals large scale chromatin reorganization and gene silencing linked to defective DNA repair
    • Baltanás, F. C., Casafont, I., Lafarga, V., Weruaga, E., Alonso, J. R., Berciano, M. T., and Lafarga, M. (2011) Purkinje cell degeneration in pcd mice reveals large scale chromatin reorganization and gene silencing linked to defective DNA repair. J. Biol. Chem. 286, 28287-28302
    • (2011) J. Biol. Chem. , vol.286 , pp. 28287-28302
    • Baltanás, F.C.1    Casafont, I.2    Lafarga, V.3    Weruaga, E.4    Alonso, J.R.5    Berciano, M.T.6    Lafarga, M.7
  • 12
    • 33244496230 scopus 로고    scopus 로고
    • Emergence of endoplasmic reticulum stress and activated microglia in Purkinje cell degeneration mice
    • DOI 10.1016/j.neulet.2005.11.023, PII S0304394005012899
    • Kyuhou, S., Kato, N., and Gemba, H. (2006) Emergence of endoplasmic reticulum stress and activated microglia in Purkinje cell degeneration mice. Neurosci. Lett. 396, 91-96 (Pubitemid 43276419)
    • (2006) Neuroscience Letters , vol.396 , Issue.2 , pp. 91-96
    • Kyuhou, S.-I.1    Kato, N.2    Gemba, H.3
  • 13
    • 0028023270 scopus 로고
    • Axonal torpedoes in cerebellar Purkinje cells of two normal mouse strains during aging
    • Bäurle, J., and Grüsser-Cornehls, U. (1994) Axonal torpedoes in cerebellar Purkinje cells of two normal mouse strains during aging. Acta Neuropathol. 88, 237-245
    • (1994) Acta Neuropathol. , vol.88 , pp. 237-245
    • Bäurle, J.1    Grüsser-Cornehls, U.2
  • 15
    • 77953495946 scopus 로고    scopus 로고
    • CCP1/Nna1 functions in protein turnover in mouse brain. Implications for cell death in Purkinje cell degeneration mice
    • Berezniuk, I., Sironi, J., Callaway, M. B., Castro, L. M., Hirata, I. Y., Ferro, E. S., and Fricker, L. D. (2010) CCP1/Nna1 functions in protein turnover in mouse brain. Implications for cell death in Purkinje cell degeneration mice. FASEB J. 24, 1813-1823
    • (2010) FASEB J. , vol.24 , pp. 1813-1823
    • Berezniuk, I.1    Sironi, J.2    Callaway, M.B.3    Castro, L.M.4    Hirata, I.Y.5    Ferro, E.S.6    Fricker, L.D.7
  • 17
    • 77953706260 scopus 로고    scopus 로고
    • A defect in cytosolic carboxypeptidase 1 (Nna1) causes autophagy in Purkinje cell degeneration mouse brain
    • Berezniuk, I., and Fricker, L. D. (2010) A defect in cytosolic carboxypeptidase 1 (Nna1) causes autophagy in Purkinje cell degeneration mouse brain. Autophagy 6, 558-559
    • (2010) Autophagy , vol.6 , pp. 558-559
    • Berezniuk, I.1    Fricker, L.D.2
  • 18
    • 77953806216 scopus 로고    scopus 로고
    • Unique post-translational modifications in specialized microtubule architecture
    • Ikegami, K., and Setou, M. (2010) Unique post-translational modifications in specialized microtubule architecture. Cell Struct. Funct. 35, 15-22
    • (2010) Cell Struct. Funct. , vol.35 , pp. 15-22
    • Ikegami, K.1    Setou, M.2
  • 19
    • 77957868249 scopus 로고    scopus 로고
    • Post-translational modifications of microtubules
    • Wloga, D., and Gaertig, J. (2010) Post-translational modifications of microtubules. J. Cell Sci. 123, 3447-3455
    • (2010) J. Cell Sci. , vol.123 , pp. 3447-3455
    • Wloga, D.1    Gaertig, J.2
  • 20
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton. Mechanisms and functions
    • Janke, C., and Bulinski, J. C. (2011) Post-translational regulation of the microtubule cytoskeleton. Mechanisms and functions. Nat. Rev. Mol. Cell Biol. 12, 773-786
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 21
    • 0017903434 scopus 로고
    • 14C] tyrosine by brain extract. Separation of a carboxypeptidase from tubulin-tyrosine ligase
    • 14C]tyrosine by brain extract. Separation of a carboxypeptidase from tubulin-tyrosine ligase. Mol. Cell. Biochem. 19, 17-21
    • (1978) Mol. Cell. Biochem. , vol.19 , pp. 17-21
    • Argaraña, C.E.1    Barra, H.S.2    Caputto, R.3
  • 22
    • 0017406215 scopus 로고
    • Enzyme which specifically adds tyrosine to the α chain of tubulin
    • Raybin, D., and Flavin, M. (1977) Enzyme that specifically adds tyrosine to the α chain of tubulin. Biochemistry 16, 2189-2194 (Pubitemid 8120887)
    • (1977) Biochemistry , vol.16 , Issue.10 , pp. 2189-2194
    • Raybin, D.1    Flavin, M.2
  • 26
    • 33750074428 scopus 로고    scopus 로고
    • TTLL7 is a mammalian β-tubulin polyglutamylase required for growth of MAP2-positive neurites
    • DOI 10.1074/jbc.M603984200
    • Ikegami, K., Mukai, M., Tsuchida, J., Heier, R. L., Macgregor, G. R., and Setou, M. (2006) TTLL7 is a mammalian β-tubulin polyglutamylase required for growth of MAP2-positive neurites. J. Biol. Chem. 281, 30707-30716 (Pubitemid 44582126)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.41 , pp. 30707-30716
    • Ikegami, K.1    Mukai, M.2    Tsuchida, J.-I.3    Heier, R.L.4    MacGregor, G.R.5    Setou, M.6
  • 27
    • 34247620196 scopus 로고    scopus 로고
    • A Targeted Multienzyme Mechanism for Selective Microtubule Polyglutamylation
    • DOI 10.1016/j.molcel.2007.04.012, PII S1097276507002481
    • van Dijk, J., Rogowski, K., Miro, J., Lacroix, B., Eddé, B., and Janke, C. (2007) A targeted multienzyme mechanism for selective microtubule polyglutamylation. Mol. Cell. 26, 437-448 (Pubitemid 46687103)
    • (2007) Molecular Cell , vol.26 , Issue.3 , pp. 437-448
    • Van Dijk, J.1    Rogowski, K.2    Miro, J.3    Lacroix, B.4    Edde, B.5    Janke, C.6
  • 30
    • 77953732642 scopus 로고    scopus 로고
    • Tubulin polyglutamylation is essential for airway ciliary function through the regulation of beating asymmetry
    • Ikegami, K., Sato, S., Nakamura, K., Ostrowski, L. E., and Setou, M. (2010) Tubulin polyglutamylation is essential for airway ciliary function through the regulation of beating asymmetry. Proc. Natl. Acad. Sci. U.S.A. 107, 10490-10495
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 10490-10495
    • Ikegami, K.1    Sato, S.2    Nakamura, K.3    Ostrowski, L.E.4    Setou, M.5
  • 31
    • 57449116568 scopus 로고    scopus 로고
    • Multiple isotopic labels for quantitative mass spectrometry
    • Morano, C., Zhang, X., and Fricker, L. D. (2008) Multiple isotopic labels for quantitative mass spectrometry. Anal. Chem. 80, 9298-9309
    • (2008) Anal. Chem. , vol.80 , pp. 9298-9309
    • Morano, C.1    Zhang, X.2    Fricker, L.D.3
  • 33
    • 77950959281 scopus 로고    scopus 로고
    • Hemopressins and other hemoglobin-derived peptides in mouse brain. Comparison between brain, blood, and heart peptidome and regulation in Cpefat/fat mice
    • Gelman, J. S., Sironi, J., Castro, L. M., Ferro, E. S., and Fricker, L. D. (2010) Hemopressins and other hemoglobin-derived peptides in mouse brain. Comparison between brain, blood, and heart peptidome and regulation in Cpefat/fat mice. J. Neurochem. 113, 871-880
    • (2010) J. Neurochem. , vol.113 , pp. 871-880
    • Gelman, J.S.1    Sironi, J.2    Castro, L.M.3    Ferro, E.S.4    Fricker, L.D.5
  • 34
    • 80054727597 scopus 로고    scopus 로고
    • Quantitative peptidomics of mice lacking peptide-processing enzymes
    • Wardman, J., and Fricker, L. D. (2011) Quantitative peptidomics of mice lacking peptide-processing enzymes. Methods Mol. Biol. 768, 307-323
    • (2011) Methods Mol. Biol. , vol.768 , pp. 307-323
    • Wardman, J.1    Fricker, L.D.2
  • 36
    • 0037177891 scopus 로고    scopus 로고
    • Identification and characterization of three members of the human metallocarboxypeptidase gene family
    • DOI 10.1074/jbc.M112254200
    • Wei, S., Segura, S., Vendrell, J., Aviles, F. X., Lanoue, E., Day, R., Feng, Y., and Fricker, L. D. (2002) Identification and characterization of three members of the human metallocarboxypeptidase gene family. J. Biol. Chem. 277, 14954-14964 (Pubitemid 34952570)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 14954-14964
    • Wei, S.1    Segura, S.2    Vendrell, J.3    Aviles, F.X.4    Lanoue, E.5    Day, R.6    Feng, Y.7    Fricker, L.D.8
  • 37
    • 33744930155 scopus 로고    scopus 로고
    • Miniaturization and validation of a sensitive multiparametric cell-based assay for the concomitant detection of microtubule-destabilizing and microtubule-stabilizing agents
    • DOI 10.1177/1087057106286210
    • Vassal, E., Barette, C., Fonrose, X., Dupont, R., Sans-Soleilhac, E., and Lafanechère, L. (2006) Miniaturization and validation of a sensitive multiparametric cell-based assay for the concomitant detection of microtubule- destabilizing and microtubule-stabilizing agents. J. Biomol. Screen. 11, 377-389 (Pubitemid 43846338)
    • (2006) Journal of Biomolecular Screening , vol.11 , Issue.4 , pp. 377-389
    • Vassal, E.1    Barette, C.2    Fonrose, X.3    Dupont, R.4    Sans-Soleilhac, E.5    Lafanechere, L.6
  • 38
    • 0001727492 scopus 로고
    • Enkephalin convertase: Purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules
    • DOI 10.1073/pnas.79.12.3886
    • Fricker, L. D., and Snyder, S. H. (1982) Enkephalin convertase. Purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules. Proc. Natl. Acad. Sci. U.S.A. 79, 3886-3890 (Pubitemid 12013561)
    • (1982) Proceedings of the National Academy of Sciences of the United States of America , vol.79 , Issue.12 I , pp. 3886-3890
    • Fricker, L.D.1    Snyder, S.H.2
  • 39
    • 0028790290 scopus 로고
    • Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary
    • Song, L., and Fricker, L. D. (1995) Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. J. Biol. Chem. 270, 25007-25013
    • (1995) J. Biol. Chem. , vol.270 , pp. 25007-25013
    • Song, L.1    Fricker, L.D.2
  • 42
    • 80655128140 scopus 로고    scopus 로고
    • Carboxypeptidase O is a glycosyl-phosphatidylinositol-anchored intestinal peptidase with acidic amino acid specificity
    • Lyons, P. J., and Fricker, L. D. (2011) Carboxypeptidase O is a glycosyl-phosphatidylinositol-anchored intestinal peptidase with acidic amino acid specificity. J. Biol. Chem. 286, 39023-39032
    • (2011) J. Biol. Chem. , vol.286 , pp. 39023-39032
    • Lyons, P.J.1    Fricker, L.D.2
  • 43
    • 0023608861 scopus 로고
    • Post-translational modification and microtubule stability
    • Schulze, E., Asai, D. J., Bulinski, J. C., and Kirschner, M. (1987) Post-translational modification and microtubule stability. J. Cell Biol. 105,2167-2177
    • (1987) J. Cell Biol. , vol.105 , pp. 2167-2177
    • Schulze, E.1    Asai, D.J.2    Bulinski, J.C.3    Kirschner, M.4
  • 45
    • 0037144838 scopus 로고    scopus 로고
    • Tetrahymena thermophila contains a conventional γ-tubulin that is differentially required for the maintenance of different microtubule-organizing centers
    • Shang, Y., Li, B., and Gorovsky, M. A. (2002) Tetrahymena thermophila contains a conventional γ-tubulin that is differentially required for the maintenance of different microtubule-organizing centers. J. Cell Biol. 158,1195-1206
    • (2002) J. Cell Biol. , vol.158 , pp. 1195-1206
    • Shang, Y.1    Li, B.2    Gorovsky, M.A.3
  • 48
    • 0028283568 scopus 로고
    • Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies
    • Paturle-Lafanechere, L., Manier, M., Trigault, N., Pirollet, F., Mazarguil,H., and Job, D. (1994) Accumulation of delta2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies. J. Cell Sci. 107 1529-1543 (Pubitemid 24198472)
    • (1994) Journal of Cell Science , vol.107 , Issue.6 , pp. 1529-1543
    • Paturle-Lafanechere, L.1    Manier, M.2    Trigault, N.3    Pirollet, F.4    Mazarguil, H.5    Job, D.6
  • 49
    • 0033491915 scopus 로고    scopus 로고
    • Polyglutamylation and polyglycylation of α- and β-tubulins during in vitro ciliated cell differentiation of human respiratory epithelial cells
    • Million, K., Larcher, J., Laoukili, J., Bourguignon, D., Marano, F., and Tournier, F. (1999) Polyglutamylation and polyglycylation of α- and β-tubulins during in vitro ciliated cell differentiation of human respiratory epithelial cells. J. Cell Sci. 112 4357-4366 (Pubitemid 30122027)
    • (1999) Journal of Cell Science , vol.112 , Issue.23 , pp. 4357-4366
    • Million, K.1    Larcher, J.-C.2    Laoukili, J.3    Bourguignon, D.4    Marano, F.5    Tournier, F.6
  • 50
    • 0032941748 scopus 로고    scopus 로고
    • Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism
    • Kreitzer, G., Liao, G., and Gundersen, G. G. (1999) Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism. Mol. Biol. Cell 10, 1105-1118 (Pubitemid 29193734)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.4 , pp. 1105-1118
    • Kreitzer, G.1    Liao, G.2    Gundersen, G.G.3
  • 51
  • 53
    • 80054995650 scopus 로고    scopus 로고
    • The tubulin deglutamylase CCPP-1 regulates the function and stability of sensory cilia in C. elegans
    • O'Hagan, R., Piasecki, B. P., Silva, M., Phirke, P., Nguyen, K. C., Hall, D. H., Swoboda, P., and Barr, M. M. (2011) The tubulin deglutamylase CCPP-1 regulates the function and stability of sensory cilia in C. elegans. Curr. Biol. 21, 1685-1694
    • (2011) Curr. Biol. , vol.21 , pp. 1685-1694
    • O'Hagan, R.1    Piasecki, B.P.2    Silva, M.3    Phirke, P.4    Nguyen, K.C.5    Hall, D.H.6    Swoboda, P.7    Barr, M.M.8
  • 54


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.