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Volumn 69, Issue , 2016, Pages 99-105

Chaperone BAG6 is dispensable for MHC class I antigen processing and presentation

Author keywords

Antigen presentation; Antigen processing; BAG6; DRiPs; MHC class I

Indexed keywords

CHAPERONE; CHAPERONE BAG6; EPITOPE; GAMMA INTERFERON; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; SMALL INTERFERING RNA; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; BAG6 PROTEIN, HUMAN; BAG6 PROTEIN, MOUSE; HLA ANTIGEN CLASS 1; NUCLEAR PROTEIN;

EID: 84948844037     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2015.11.004     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 0025261931 scopus 로고
    • A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domain
    • Banerji, J., Sands, J., Strominger, J.L., Spies, T., A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domain. Proc. Natl. Acad. Sci. U. S. A. 87 (1990), 2374–2378.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 2374-2378
    • Banerji, J.1    Sands, J.2    Strominger, J.L.3    Spies, T.4
  • 2
    • 4644249095 scopus 로고    scopus 로고
    • Immunoproteasomes down-regulate presentation of a subdominant T cell epitope from lymphocytic choriomeningitis virus
    • Basler, M., Youhnovski, N., van den Broek, M., Przybylski, M., Groettrup, M., Immunoproteasomes down-regulate presentation of a subdominant T cell epitope from lymphocytic choriomeningitis virus. J. Immunol. 173 (2004), 3925–3934.
    • (2004) J. Immunol. , vol.173 , pp. 3925-3934
    • Basler, M.1    Youhnovski, N.2    van den Broek, M.3    Przybylski, M.4    Groettrup, M.5
  • 3
    • 84899080404 scopus 로고    scopus 로고
    • The nature and extent of contributions by defective ribosome products to the HLA peptidome
    • Bourdetsky, D., Schmelzer, C.E., Admon, A., The nature and extent of contributions by defective ribosome products to the HLA peptidome. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), 1591–1599.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 1591-1599
    • Bourdetsky, D.1    Schmelzer, C.E.2    Admon, A.3
  • 5
    • 82955207151 scopus 로고    scopus 로고
    • BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum
    • Claessen, J.H., Ploegh, H.L., BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum. PLoS One, 6, 2011, e28542.
    • (2011) PLoS One , vol.6 , pp. e28542
    • Claessen, J.H.1    Ploegh, H.L.2
  • 6
    • 84896950126 scopus 로고    scopus 로고
    • The chaperone BAG6 captures dislocated glycoproteins in the cytosol
    • Claessen, J.H., Sanyal, S., Ploegh, H.L., The chaperone BAG6 captures dislocated glycoproteins in the cytosol. PLoS One, 9, 2014, e90204.
    • (2014) PLoS One , vol.9 , pp. e90204
    • Claessen, J.H.1    Sanyal, S.2    Ploegh, H.L.3
  • 9
    • 79960637590 scopus 로고    scopus 로고
    • Protein targeting and degradation are coupled for elimination of mislocalized proteins
    • Hessa, T., Sharma, A., Mariappan, M., Eshleman, H.D., Gutierrez, E., Hegde, R.S., Protein targeting and degradation are coupled for elimination of mislocalized proteins. Nature 475 (2011), 394–397.
    • (2011) Nature , vol.475 , pp. 394-397
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5    Hegde, R.S.6
  • 10
    • 0034756104 scopus 로고    scopus 로고
    • From the cradle to the grave: molecular chaperones that may choose between folding and degradation
    • Hohfeld, J., Cyr, D.M., Patterson, C., From the cradle to the grave: molecular chaperones that may choose between folding and degradation. EMBO Rep. 2 (2001), 885–890.
    • (2001) EMBO Rep. , vol.2 , pp. 885-890
    • Hohfeld, J.1    Cyr, D.M.2    Patterson, C.3
  • 11
    • 84874506372 scopus 로고    scopus 로고
    • Hsp90: structure and function
    • Jackson, S.E., Hsp90: structure and function. Top. Curr. Chem. 328 (2013), 155–240.
    • (2013) Top. Curr. Chem. , vol.328 , pp. 155-240
    • Jackson, S.E.1
  • 12
    • 0033854292 scopus 로고    scopus 로고
    • Assembly, target-signaling and intracellular transport of tyrosinase gene family proteins in the initial stage of melanosome biogenesis
    • Jimbow, K., Park, J.S., Kato, F., Hirosaki, K., Toyofuku, K., Hua, C., Yamashita, T., Assembly, target-signaling and intracellular transport of tyrosinase gene family proteins in the initial stage of melanosome biogenesis. Pigment Cell Res. 13 (2000), 222–229.
    • (2000) Pigment Cell Res. , vol.13 , pp. 222-229
    • Jimbow, K.1    Park, J.S.2    Kato, F.3    Hirosaki, K.4    Toyofuku, K.5    Hua, C.6    Yamashita, T.7
  • 13
    • 84855367971 scopus 로고    scopus 로고
    • Gamma-Interferon-regulated chaperone governs human lymphocyte antigen class II expression
    • Kamper, N., Franken, S., Temme, S., Koch, S., Bieber, T., Koch, N., Gamma-Interferon-regulated chaperone governs human lymphocyte antigen class II expression. FASEB J. 26 (2012), 104–116.
    • (2012) FASEB J. , vol.26 , pp. 104-116
    • Kamper, N.1    Franken, S.2    Temme, S.3    Koch, S.4    Bieber, T.5    Koch, N.6
  • 14
    • 84878191743 scopus 로고    scopus 로고
    • BAG6/BAT3: emerging roles in quality control for nascent polypeptides
    • Kawahara, H., Minami, R., Yokota, N., BAG6/BAT3: emerging roles in quality control for nascent polypeptides. J. Biochem. 153 (2013), 147–160.
    • (2013) J. Biochem. , vol.153 , pp. 147-160
    • Kawahara, H.1    Minami, R.2    Yokota, N.3
  • 15
    • 0035500453 scopus 로고    scopus 로고
    • Cutting edge: neosynthesis is required for the presentation of a T cell epitope from a long-lived viral protein
    • Khan, S., de Giuli, R., Schmidtke, G., Bruns, M., Buchmeier, M., van den Broek, M., Groettrup, M., Cutting edge: neosynthesis is required for the presentation of a T cell epitope from a long-lived viral protein. J. Immunol. 167 (2001), 4801–4804.
    • (2001) J. Immunol. , vol.167 , pp. 4801-4804
    • Khan, S.1    de Giuli, R.2    Schmidtke, G.3    Bruns, M.4    Buchmeier, M.5    van den Broek, M.6    Groettrup, M.7
  • 16
    • 66849109240 scopus 로고    scopus 로고
    • The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
    • Kramer, G., Boehringer, D., Ban, N., Bukau, B., The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat. Struct. Mol. Biol. 16 (2009), 589–597.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 589-597
    • Kramer, G.1    Boehringer, D.2    Ban, N.3    Bukau, B.4
  • 17
    • 84874976264 scopus 로고    scopus 로고
    • Bag6/Bat3/Scythe: a novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation
    • Lee, J.G., Ye, Y., Bag6/Bat3/Scythe: a novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation. Bioessays 35 (2013), 377–385.
    • (2013) Bioessays , vol.35 , pp. 377-385
    • Lee, J.G.1    Ye, Y.2
  • 19
    • 77954352789 scopus 로고    scopus 로고
    • Bat3 promotes the membrane integration of tail-anchored proteins
    • Leznicki, P., Clancy, A., Schwappach, B., High, S., Bat3 promotes the membrane integration of tail-anchored proteins. J. Cell Sci. 123 (2010), 2170–2178.
    • (2010) J. Cell Sci. , vol.123 , pp. 2170-2178
    • Leznicki, P.1    Clancy, A.2    Schwappach, B.3    High, S.4
  • 22
    • 77955878748 scopus 로고    scopus 로고
    • BAG-6 is essential for selective elimination of defective proteasomal substrates
    • Minami, R., Hayakawa, A., Kagawa, H., Yanagi, Y., Yokosawa, H., Kawahara, H., BAG-6 is essential for selective elimination of defective proteasomal substrates. J. Cell Biol. 190 (2010), 637–650.
    • (2010) J. Cell Biol. , vol.190 , pp. 637-650
    • Minami, R.1    Hayakawa, A.2    Kagawa, H.3    Yanagi, Y.4    Yokosawa, H.5    Kawahara, H.6
  • 23
    • 0029968531 scopus 로고    scopus 로고
    • Importance of MHC class 1 alpha2 and alpha3 domains in the recognition of self and non-self MHC molecules
    • Newberg, M.H., Smith, D.H., Haertel, S.B., Vining, D.R., Lacy, E., Engelhard, V.H., Importance of MHC class 1 alpha2 and alpha3 domains in the recognition of self and non-self MHC molecules. J. Immunol. 156 (1996), 2473–2480.
    • (1996) J. Immunol. , vol.156 , pp. 2473-2480
    • Newberg, M.H.1    Smith, D.H.2    Haertel, S.B.3    Vining, D.R.4    Lacy, E.5    Engelhard, V.H.6
  • 25
    • 84903780276 scopus 로고    scopus 로고
    • BAG6 regulates the quality control of a polytopic ERAD substrate
    • Payapilly, A., High, S., BAG6 regulates the quality control of a polytopic ERAD substrate. J. Cell Sci. 127 (2014), 2898–2909.
    • (2014) J. Cell Sci. , vol.127 , pp. 2898-2909
    • Payapilly, A.1    High, S.2
  • 26
    • 0034624961 scopus 로고    scopus 로고
    • Tyrosinase and glycoprotein folding: roles of chaperones that recognize glycans
    • Petrescu, S.M., Branza-Nichita, N., Negroiu, G., Petrescu, A.J., Dwek, R.A., Tyrosinase and glycoprotein folding: roles of chaperones that recognize glycans. Biochemistry 39 (2000), 5229–5237.
    • (2000) Biochemistry , vol.39 , pp. 5229-5237
    • Petrescu, S.M.1    Branza-Nichita, N.2    Negroiu, G.3    Petrescu, A.J.4    Dwek, R.A.5
  • 27
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I- and type-II-interferon-mediated signalling
    • Platanias, L.C., Mechanisms of type-I- and type-II-interferon-mediated signalling. Nat. Rev. Immunol. 5 (2005), 375–386.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 28
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock, K.L., Goldberg, A.L., Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17 (1999), 739–779.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 29
    • 84904567733 scopus 로고    scopus 로고
    • Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6
    • Rodrigo-Brenni, M.C., Gutierrez, E., Hegde, R.S., Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6. Mol. Cell 55 (2014), 227–237.
    • (2014) Mol. Cell , vol.55 , pp. 227-237
    • Rodrigo-Brenni, M.C.1    Gutierrez, E.2    Hegde, R.S.3
  • 30
    • 84869065405 scopus 로고    scopus 로고
    • Design principles of protein biosynthesis-coupled quality control
    • Rodrigo-Brenni, M.C., Hegde, R.S., Design principles of protein biosynthesis-coupled quality control. Dev. Cell 23 (2012), 896–907.
    • (2012) Dev. Cell , vol.23 , pp. 896-907
    • Rodrigo-Brenni, M.C.1    Hegde, R.S.2
  • 31
    • 0041026092 scopus 로고    scopus 로고
    • Interaction of Hsp70 chaperones with substrates
    • Rudiger, S., Buchberger, A., Bukau, B., Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol. 4 (1997), 342–349.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 342-349
    • Rudiger, S.1    Buchberger, A.2    Bukau, B.3
  • 32
    • 0026739463 scopus 로고
    • The interferon system. A bird's eye view of its biochemistry
    • Sen, G.C., Lengyel, P., The interferon system. A bird's eye view of its biochemistry. J. Biol. Chem. 267 (1992), 5017–5020.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5017-5020
    • Sen, G.C.1    Lengyel, P.2
  • 34
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation
    • Wang, Q., Liu, Y., Soetandyo, N., Baek, R., Hegde, R.S., A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Mol. Cell 42 (2011), 758–770.
    • (2011) Mol. Cell , vol.42 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, R.4    Hegde, R.S.5
  • 35
    • 0028095394 scopus 로고
    • The human BAT3 ortholog in rodents is predominantly and developmentally expressed in testis
    • Wang, R., Liew, C.C., The human BAT3 ortholog in rodents is predominantly and developmentally expressed in testis. Mol. Cell. Biochem. 136 (1994), 49–57.
    • (1994) Mol. Cell. Biochem. , vol.136 , pp. 49-57
    • Wang, R.1    Liew, C.C.2
  • 36
    • 0030239693 scopus 로고    scopus 로고
    • Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules?
    • Yewdell, J.W., Anton, L.C., Bennink, J.R., Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules?. J. Immunol. 157 (1996), 1823–1826.
    • (1996) J. Immunol. , vol.157 , pp. 1823-1826
    • Yewdell, J.W.1    Anton, L.C.2    Bennink, J.R.3
  • 37
    • 33745833084 scopus 로고    scopus 로고
    • The DRiP hypothesis decennial: support, controversy, refinement and extension
    • Yewdell, J.W., Nicchitta, C.V., The DRiP hypothesis decennial: support, controversy, refinement and extension. Trends Immunol. 27 (2006), 368–373.
    • (2006) Trends Immunol. , vol.27 , pp. 368-373
    • Yewdell, J.W.1    Nicchitta, C.V.2


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