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Volumn 130, Issue 19, 2017, Pages 3234-3247

A genome-wide CRISPR screen reconciles the role of N-linked glycosylation in galectin-3 transport to the cell surface

Author keywords

Galectin; Glycosylation; Unconventional secretion

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR ALPHA1; ADAM10 ENDOPEPTIDASE; APLP2 PROTEIN; ARTN PROTEIN; C2 PROTEIN; CD302 PROTEIN; CD33 ANTIGEN; CHRM4 PROTEIN; CLCA1 PROTEIN; CTNND2 PROTEIN; DSG3 PROTEIN; FAP PROTEIN; FGF17 PROTEIN; FRAS1 PROTEIN; GALECTIN 3; GIF PROTEIN; GLYCOPROTEIN; HIST1H2BD PROTEIN; HS6ST2 PROTEIN; INTERLEUKIN 27; ITGB3 PROTEIN; LAMB2 PROTEIN; LUM PROTEIN; MAN1A2 PROTEIN; MPZL3 PROTEIN; MULTIDRUG RESISTANCE ASSOCIATED PROTEIN 3; NDST2 PROTEIN; NHLRC3 PROTEIN; NPR1 PROTEIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; GALECTIN-3, HUMAN;

EID: 85030530681     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.206425     Document Type: Article
Times cited : (33)

References (54)
  • 2
    • 85030555093 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: a review
    • Albahri, Z. (2015) Congenital disorders of glycosylation: a review. Am. J. Pediatr. 1, 6-28
    • (2015) Am. J. Pediatr , vol.1 , pp. 6-28
    • Albahri, Z.1
  • 3
    • 84881552168 scopus 로고    scopus 로고
    • The role of 'eat-me' signals and autophagy cargo receptors in innate immunity
    • Boyle, K. B. and Randow, F. (2013) The role of 'eat-me' signals and autophagy cargo receptors in innate immunity. Curr. Opin. Microbiol. 16, 339-348
    • (2013) Curr. Opin. Microbiol , vol.16 , pp. 339-348
    • Boyle, K.B.1    Randow, F.2
  • 4
    • 84917725056 scopus 로고    scopus 로고
    • Easy quantitative assessment of genome editing by sequence trace decomposition
    • Brinkman, E. K., Chen, T., Amendola, M. and van Steensel, B. (2014) Easy quantitative assessment of genome editing by sequence trace decomposition. Nucleic Acids Res. 42, e168
    • (2014) Nucleic Acids Res , vol.42
    • Brinkman, E.K.1    Chen, T.2    Amendola, M.3    van Steensel, B.4
  • 5
    • 84992645517 scopus 로고    scopus 로고
    • TRIMs and galectins globally cooperate and TRIM16 and galectin-3 co-direct autophagy in endomembrane damage homeostasis
    • Chauhan, S., Kumar, S., Jain, A., Ponpuak, M., Mudd, M. H., Kimura, T., Choi, S. W., Peters, R., Mandell, M., Bruun, J.-A. et al. (2016) TRIMs and galectins globally cooperate and TRIM16 and galectin-3 co-direct autophagy in endomembrane damage homeostasis. Dev. Cell 39, 13-27
    • (2016) Dev. Cell , vol.39 , pp. 13-27
    • Chauhan, S.1    Kumar, S.2    Jain, A.3    Ponpuak, M.4    Mudd, M.H.5    Kimura, T.6    Choi, S.W.7    Peters, R.8    Mandell, M.9    Bruun, J.-A.10
  • 6
    • 0037234471 scopus 로고    scopus 로고
    • Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I
    • Chen, W. and Stanley, P. (2003) Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I. Glycobiology 13, 43-50
    • (2003) Glycobiology , vol.13 , pp. 43-50
    • Chen, W.1    Stanley, P.2
  • 7
    • 0028986607 scopus 로고
    • Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. II. Localization and biosynthesis
    • Cho, M. and Cummings, R. D. (1995) Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. II. Localization and biosynthesis. J. Biol. Chem. 270, 5207-5212
    • (1995) J. Biol. Chem , vol.270 , pp. 5207-5212
    • Cho, M.1    Cummings, R.D.2
  • 8
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism
    • Cooper, D. N. and Barondes, S. H. (1990) Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J. Cell Biol. 110, 1681-1691
    • (1990) J. Cell Biol , vol.110 , pp. 1681-1691
    • Cooper, D.N.1    Barondes, S.H.2
  • 9
    • 34447265020 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4
    • Crump, C. M., Yates, C. and Minson, T. (2007) Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4. J. Virol. 81, 7380-7387
    • (2007) J. Virol , vol.81 , pp. 7380-7387
    • Crump, C.M.1    Yates, C.2    Minson, T.3
  • 10
    • 84936774693 scopus 로고    scopus 로고
    • Assembly, organization and regulation of cell-surface receptors by lectinglycan complexes
    • Elola, M. T., Blidner, A. G., Ferragut, F., Bracalente, C. and Rabinovich, G. A. (2015) Assembly, organization and regulation of cell-surface receptors by lectinglycan complexes. Biochem. J. 469, 1-16
    • (2015) Biochem. J , vol.469 , pp. 1-16
    • Elola, M.T.1    Blidner, A.G.2    Ferragut, F.3    Bracalente, C.4    Rabinovich, G.A.5
  • 11
    • 0032493658 scopus 로고    scopus 로고
    • Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human Blymphocytes
    • Escola, J.-M., Kleijmeer, M. J., Stoorvogel, W., Griffith, J. M., Yoshie, O. and Geuze, H. J. (1998) Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human Blymphocytes. J. Biol. Chem. 273, 20121-20127
    • (1998) J. Biol. Chem , vol.273 , pp. 20121-20127
    • Escola, J.-M.1    Kleijmeer, M.J.2    Stoorvogel, W.3    Griffith, J.M.4    Yoshie, O.5    Geuze, H.J.6
  • 14
    • 0036840817 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: a review
    • Grünewald, S., Matthijs, G. and Jaeken, J. (2002) Congenital disorders of glycosylation: a review. Pediatr. Res. 52, 618-624
    • (2002) Pediatr. Res , vol.52 , pp. 618-624
    • Grünewald, S.1    Matthijs, G.2    Jaeken, J.3
  • 15
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang, W., Sherman, B. T. and Lempicki, R. A. (2009a). Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 37, 1-13
    • (2009) Nucleic Acids Res , vol.37 , pp. 1-13
    • Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 16
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang, W., Sherman, B. T. and Lempicki, R. A. (2009b). Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44-57
    • (2009) Nat. Protoc , vol.4 , pp. 44-57
    • Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 17
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydratebinding proteins
    • Hughes, R. C. (1999) Secretion of the galectin family of mammalian carbohydratebinding proteins. Biochim. Biophys. Acta 1473, 172-185
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 20
    • 0024408670 scopus 로고
    • Transfection of a human gene that corrects the Lec1 glycosylation defect: evidence for transfer of the structural gene for Nacetylglucosaminyltransferase I
    • Kumar, R. and Stanley, P. (1989) Transfection of a human gene that corrects the Lec1 glycosylation defect: evidence for transfer of the structural gene for Nacetylglucosaminyltransferase I. Mol. Cell. Biol. 9, 5713-5717
    • (1989) Mol. Cell. Biol , vol.9 , pp. 5713-5717
    • Kumar, R.1    Stanley, P.2
  • 22
    • 0027212532 scopus 로고
    • Apical secretion of a cytosolic protein by Madin-Darby canine kidney cells Evidence for polarized release of an endogenous lectin by a nonclassical secretory pathway
    • Lindstedt, R., Apodaca, G., Barondes, S. H., Mostov, K. E. and Leffler, H. (1993) Apical secretion of a cytosolic protein by Madin-Darby canine kidney cells. Evidence for polarized release of an endogenous lectin by a nonclassical secretory pathway. J. Biol. Chem. 268, 11750-11757
    • (1993) J. Biol. Chem , vol.268 , pp. 11750-11757
    • Lindstedt, R.1    Apodaca, G.2    Barondes, S.H.3    Mostov, K.E.4    Leffler, H.5
  • 23
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • Liu, F.-T. and Rabinovich, G. A. (2005) Galectins as modulators of tumour progression. Nat. Rev. Cancer 5, 29-41
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 29-41
    • Liu, F.-T.1    Rabinovich, G.A.2
  • 25
    • 84857048734 scopus 로고    scopus 로고
    • Cell-surface galectin-3 confers resistance to TRAIL by impeding trafficking of death receptors in metastatic colon adenocarcinoma cells
    • Mazurek, N., Byrd, J. C., Sun, Y., Hafley, M., Ramirez, K., Burks, J. and Bresalier, R. S. (2012) Cell-surface galectin-3 confers resistance to TRAIL by impeding trafficking of death receptors in metastatic colon adenocarcinoma cells. Cell Death Differ. 19, 523-533
    • (2012) Cell Death Differ , vol.19 , pp. 523-533
    • Mazurek, N.1    Byrd, J.C.2    Sun, Y.3    Hafley, M.4    Ramirez, K.5    Burks, J.6    Bresalier, R.S.7
  • 26
    • 84992154214 scopus 로고    scopus 로고
    • Galectin-3 in patients with chronic heart failure: association with oxidative stress, inflammation, renal dysfunction and prognosis
    • Medvedeva, E. A., Berezin, I. I., Surkova, E. A., Yaranov, D. M. and Shchukin, Y. V. (2016) Galectin-3 in patients with chronic heart failure: association with oxidative stress, inflammation, renal dysfunction and prognosis. Minerva Cardioangiol. 64, 595-602
    • (2016) Minerva Cardioangiol , vol.64 , pp. 595-602
    • Medvedeva, E.A.1    Berezin, I.I.2    Surkova, E.A.3    Yaranov, D.M.4    Shchukin, Y.V.5
  • 27
    • 0030994878 scopus 로고    scopus 로고
    • Plasma membrane targetting, vesicular budding and release of galectin 3 from the cytoplasm of mammalian cells during secretion
    • Mehul, B. and Hughes, R. C. (1997) Plasma membrane targetting, vesicular budding and release of galectin 3 from the cytoplasm of mammalian cells during secretion. J. Cell Sci. 110, 1169-1178
    • (1997) J. Cell Sci , vol.110 , pp. 1169-1178
    • Mehul, B.1    Hughes, R.C.2
  • 28
    • 0033199579 scopus 로고    scopus 로고
    • Determinants in the N-terminal domains of galectin-3 for secretion by a novel pathway circumventing the endoplasmic reticulum-Golgi complex
    • Menon, R. P. and Hughes, R. C. (1999) Determinants in the N-terminal domains of galectin-3 for secretion by a novel pathway circumventing the endoplasmic reticulum-Golgi complex. Eur. J. Biochem. 264, 569-576
    • (1999) Eur. J. Biochem , vol.264 , pp. 569-576
    • Menon, R.P.1    Hughes, R.C.2
  • 30
    • 84935505241 scopus 로고    scopus 로고
    • The galectin lattice at a glance
    • Nabi, I. R., Shankar, J. and Dennis, J. W. (2015) The galectin lattice at a glance. J. Cell Sci. 128, 2213-2219
    • (2015) J. Cell Sci , vol.128 , pp. 2213-2219
    • Nabi, I.R.1    Shankar, J.2    Dennis, J.W.3
  • 31
    • 85009198548 scopus 로고    scopus 로고
    • Atg8 family LC3/GABARAP proteins are crucial for autophagosomelysosome fusion but not autophagosome formation during PINK1/Parkin mitophagy and starvation
    • Nguyen, T. N., Padman, B. S., Usher, J., Oorschot, V., Ramm, G. and Lazarou, M. (2016) Atg8 family LC3/GABARAP proteins are crucial for autophagosomelysosome fusion but not autophagosome formation during PINK1/Parkin mitophagy and starvation. J. Cell Biol. 215, 857-874
    • (2016) J. Cell Biol , vol.215 , pp. 857-874
    • Nguyen, T.N.1    Padman, B.S.2    Usher, J.3    Oorschot, V.4    Ramm, G.5    Lazarou, M.6
  • 32
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion A current view on cargo proteins and potential export routes
    • Nickel, W. (2003) The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur. J. Biochem. 270, 2109-2119
    • (2003) Eur. J. Biochem , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 33
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W. and Rabouille, C. (2009) Mechanisms of regulated unconventional protein secretion. Nat. Rev. Mol. Cell Biol. 10, 148-155
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 34
    • 55849145075 scopus 로고    scopus 로고
    • Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells
    • Nickel, W. and Seedorf, M. (2008) Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells. Annu. Rev. Cell Dev. Biol. 24, 287-308
    • (2008) Annu. Rev. Cell Dev. Biol , vol.24 , pp. 287-308
    • Nickel, W.1    Seedorf, M.2
  • 35
    • 33751002037 scopus 로고    scopus 로고
    • Lectin-resistant CHO glycosylation mutants
    • Patnaik, S. K. and Stanley, P. (2006) Lectin-resistant CHO glycosylation mutants. Methods Enzymol. 416, 159-182
    • (2006) Methods Enzymol , vol.416 , pp. 159-182
    • Patnaik, S.K.1    Stanley, P.2
  • 36
    • 33645102970 scopus 로고    scopus 로고
    • Complex N-glycans are the major ligands for galectin-1,-3, and-8 on Chinese hamster ovary cells
    • Patnaik, S. K., Potvin, B., Carlsson, S., Sturm, D., Leffler, H. and Stanley, P. (2006) Complex N-glycans are the major ligands for galectin-1,-3, and-8 on Chinese hamster ovary cells. Glycobiology 16, 305-317
    • (2006) Glycobiology , vol.16 , pp. 305-317
    • Patnaik, S.K.1    Potvin, B.2    Carlsson, S.3    Sturm, D.4    Leffler, H.5    Stanley, P.6
  • 38
    • 84940449986 scopus 로고    scopus 로고
    • Glycosylation in cancer: mechanisms and clinical implications
    • Pinho, S. S. and Reis, C. A. (2015) Glycosylation in cancer: mechanisms and clinical implications. Nat. Rev. Cancer 15, 540-555
    • (2015) Nat. Rev. Cancer , vol.15 , pp. 540-555
    • Pinho, S.S.1    Reis, C.A.2
  • 40
    • 0036587663 scopus 로고    scopus 로고
    • Unlocking the secrets of galectins: a challenge at the frontier of glyco-immunology
    • Rabinovich, G. A., Rubinstein, N. and Fainboim, L. (2002) Unlocking the secrets of galectins: a challenge at the frontier of glyco-immunology. J. Leukoc. Biol. 71, 741-752
    • (2002) J. Leukoc. Biol , vol.71 , pp. 741-752
    • Rabinovich, G.A.1    Rubinstein, N.2    Fainboim, L.3
  • 41
    • 85007564150 scopus 로고    scopus 로고
    • Pathways of unconventional protein secretion
    • Rabouille, C. (2017) Pathways of unconventional protein secretion. Trends Cell Biol. 27, 230-240
    • (2017) Trends Cell Biol , vol.27 , pp. 230-240
    • Rabouille, C.1
  • 43
    • 0017930809 scopus 로고
    • A method for obtaining digital signatures and public-key cryptosystems
    • Rivest, R. L., Shamir, A. and Adleman, L. (1978) A method for obtaining digital signatures and public-key cryptosystems. Commun. ACM 21, 120-126
    • (1978) Commun. ACM , vol.21 , pp. 120-126
    • Rivest, R.L.1    Shamir, A.2    Adleman, L.3
  • 45
    • 84905262730 scopus 로고    scopus 로고
    • Improved vectors and genomewide libraries for CRISPR screening
    • Sanjana, N. E., Shalem, O. and Zhang, F. (2014) Improved vectors and genomewide libraries for CRISPR screening. Nat. Methods 11, 783-784
    • (2014) Nat. Methods , vol.11 , pp. 783-784
    • Sanjana, N.E.1    Shalem, O.2    Zhang, F.3
  • 46
    • 0027225381 scopus 로고
    • Secretion of the baby hamster kidney 30-kDa galactose-binding lectin from polarized and nonpolarized cells: a pathway independent of the endoplasmic reticulum-Golgi complex
    • Sato, S., Burdett, I. and Hughes, R. C. (1993) Secretion of the baby hamster kidney 30-kDa galactose-binding lectin from polarized and nonpolarized cells: a pathway independent of the endoplasmic reticulum-Golgi complex. Exp. Cell Res. 207, 8-18
    • (1993) Exp. Cell Res , vol.207 , pp. 8-18
    • Sato, S.1    Burdett, I.2    Hughes, R.C.3
  • 47
    • 27544483286 scopus 로고    scopus 로고
    • Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1
    • Seelenmeyer, C., Wegehingel, S., Tews, I., Künzler, M., Aebi, M. and Nickel, W. (2005) Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1. J. Cell Biol. 171, 373-381
    • (2005) J. Cell Biol , vol.171 , pp. 373-381
    • Seelenmeyer, C.1    Wegehingel, S.2    Tews, I.3    Künzler, M.4    Aebi, M.5    Nickel, W.6
  • 48
    • 41449107062 scopus 로고    scopus 로고
    • Unconventional secretion of fibroblast growth factor 2 and galectin-1 does not require shedding of plasma membrane-derived vesicles
    • Seelenmeyer, C., Stegmayer, C. and Nickel,W. (2008) Unconventional secretion of fibroblast growth factor 2 and galectin-1 does not require shedding of plasma membrane-derived vesicles. FEBS Lett. 582, 1362-1368
    • (2008) FEBS Lett , vol.582 , pp. 1362-1368
    • Seelenmeyer, C.1    Stegmayer, C.2    Nickel, W.3
  • 50
    • 0024559003 scopus 로고
    • Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity
    • Stanley, P. (1989) Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity. Mol. Cell. Biol. 9, 377-383
    • (1989) Mol. Cell. Biol , vol.9 , pp. 377-383
    • Stanley, P.1
  • 51
    • 84948728185 scopus 로고    scopus 로고
    • Galectin expression in cancer diagnosis and prognosis: A systematic review
    • Thijssen, V. L., Heusschen, R., Caers, J. and Griffioen, A. W. (2015) Galectin expression in cancer diagnosis and prognosis: A systematic review. Biochim. Biophys. Acta 1855, 235-247
    • (2015) Biochim. Biophys. Acta , vol.1855 , pp. 235-247
    • Thijssen, V.L.1    Heusschen, R.2    Caers, J.3    Griffioen, A.W.4
  • 54
    • 84922233366 scopus 로고    scopus 로고
    • Role of the interaction between galectin-3 and cell adhesion molecules in cancer metastasis
    • Xin, M., Dong, X.-W. and Guo, X.-L. (2015) Role of the interaction between galectin-3 and cell adhesion molecules in cancer metastasis. Biomed. Pharmacother. 69, 179-185
    • (2015) Biomed. Pharmacother , vol.69 , pp. 179-185
    • Xin, M.1    Dong, X.-W.2    Guo, X.-L.3


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