Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain

The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian...
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Autor*in:	Zhou, Yuanyuan [verfasserIn] Fan, Fenggui [verfasserIn] Han, Yongfeng [verfasserIn] Lu, Dongping [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	AtPDI11 Calreticulin 1 Endoplasmic reticulum Arabidopsis

Übergeordnetes Werk:	Enthalten in: Biochemical and biophysical research communications - Orlando, Fla. : Academic Press, 1959, 588, Seite 55-60
Übergeordnetes Werk:	volume:588 ; pages:55-60

DOI / URN:	10.1016/j.bbrc.2021.12.045

Katalog-ID:	ELV007206550

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245	1	0	\|a Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain
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520			\|a The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER.
650		4	\|a AtPDI11
650		4	\|a Calreticulin 1
650		4	\|a Endoplasmic reticulum
650		4	\|a Arabidopsis
700	1		\|a Fan, Fenggui \|e verfasserin \|4 aut
700	1		\|a Han, Yongfeng \|e verfasserin \|4 aut
700	1		\|a Lu, Dongping \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Biochemical and biophysical research communications \|d Orlando, Fla. : Academic Press, 1959 \|g 588, Seite 55-60 \|h Online-Ressource \|w (DE-627)254231691 \|w (DE-600)1461396-7 \|w (DE-576)103373039 \|x 0006-291X \|7 nnns
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912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
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936	b	k	\|a 35.70 \|j Biochemie: Allgemeines
936	b	k	\|a 42.12 \|j Biophysik
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952			\|d 588 \|h 55-60

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author_variant	y z yz f f ff y h yh d l dl
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bklnumber	35.70 42.12
publishDate	2021
allfields	10.1016/j.bbrc.2021.12.045 doi (DE-627)ELV007206550 (ELSEVIER)S0006-291X(21)01680-6 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Zhou, Yuanyuan verfasserin (orcid)0000-0001-5688-9804 aut Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER. AtPDI11 Calreticulin 1 Endoplasmic reticulum Arabidopsis Fan, Fenggui verfasserin aut Han, Yongfeng verfasserin aut Lu, Dongping verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 588, Seite 55-60 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:588 pages:55-60 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 588 55-60
spelling	10.1016/j.bbrc.2021.12.045 doi (DE-627)ELV007206550 (ELSEVIER)S0006-291X(21)01680-6 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Zhou, Yuanyuan verfasserin (orcid)0000-0001-5688-9804 aut Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER. AtPDI11 Calreticulin 1 Endoplasmic reticulum Arabidopsis Fan, Fenggui verfasserin aut Han, Yongfeng verfasserin aut Lu, Dongping verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 588, Seite 55-60 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:588 pages:55-60 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 588 55-60
allfields_unstemmed	10.1016/j.bbrc.2021.12.045 doi (DE-627)ELV007206550 (ELSEVIER)S0006-291X(21)01680-6 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Zhou, Yuanyuan verfasserin (orcid)0000-0001-5688-9804 aut Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER. AtPDI11 Calreticulin 1 Endoplasmic reticulum Arabidopsis Fan, Fenggui verfasserin aut Han, Yongfeng verfasserin aut Lu, Dongping verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 588, Seite 55-60 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:588 pages:55-60 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 588 55-60
allfieldsGer	10.1016/j.bbrc.2021.12.045 doi (DE-627)ELV007206550 (ELSEVIER)S0006-291X(21)01680-6 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Zhou, Yuanyuan verfasserin (orcid)0000-0001-5688-9804 aut Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER. AtPDI11 Calreticulin 1 Endoplasmic reticulum Arabidopsis Fan, Fenggui verfasserin aut Han, Yongfeng verfasserin aut Lu, Dongping verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 588, Seite 55-60 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:588 pages:55-60 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 588 55-60
allfieldsSound	10.1016/j.bbrc.2021.12.045 doi (DE-627)ELV007206550 (ELSEVIER)S0006-291X(21)01680-6 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Zhou, Yuanyuan verfasserin (orcid)0000-0001-5688-9804 aut Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER. AtPDI11 Calreticulin 1 Endoplasmic reticulum Arabidopsis Fan, Fenggui verfasserin aut Han, Yongfeng verfasserin aut Lu, Dongping verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 588, Seite 55-60 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:588 pages:55-60 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 588 55-60
language	English
source	Enthalten in Biochemical and biophysical research communications 588, Seite 55-60 volume:588 pages:55-60
sourceStr	Enthalten in Biochemical and biophysical research communications 588, Seite 55-60 volume:588 pages:55-60
format_phy_str_mv	Article
bklname	Biochemie: Allgemeines Biophysik
institution	findex.gbv.de
topic_facet	AtPDI11 Calreticulin 1 Endoplasmic reticulum Arabidopsis
dewey-raw	570
isfreeaccess_bool	false
container_title	Biochemical and biophysical research communications
authorswithroles_txt_mv	Zhou, Yuanyuan @@aut@@ Fan, Fenggui @@aut@@ Han, Yongfeng @@aut@@ Lu, Dongping @@aut@@
publishDateDaySort_date	2021-01-01T00:00:00Z
hierarchy_top_id	254231691
dewey-sort	3570
id	ELV007206550
language_de	englisch
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author	Zhou, Yuanyuan
spellingShingle	Zhou, Yuanyuan ddc 570 fid BIODIV bkl 35.70 bkl 42.12 misc AtPDI11 misc Calreticulin 1 misc Endoplasmic reticulum misc Arabidopsis Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain
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topic_title	570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain AtPDI11 Calreticulin 1 Endoplasmic reticulum Arabidopsis
topic	ddc 570 fid BIODIV bkl 35.70 bkl 42.12 misc AtPDI11 misc Calreticulin 1 misc Endoplasmic reticulum misc Arabidopsis
topic_unstemmed	ddc 570 fid BIODIV bkl 35.70 bkl 42.12 misc AtPDI11 misc Calreticulin 1 misc Endoplasmic reticulum misc Arabidopsis
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title	Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain
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title_full	Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain
author_sort	Zhou, Yuanyuan
journal	Biochemical and biophysical research communications
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author_browse	Zhou, Yuanyuan Fan, Fenggui Han, Yongfeng Lu, Dongping
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title_sort	arabidopsis pdi11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its d domain
title_auth	Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain
abstract	The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER.
abstractGer	The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER.
abstract_unstemmed	The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER.
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title_short	Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain
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author2	Fan, Fenggui Han, Yongfeng Lu, Dongping
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doi_str	10.1016/j.bbrc.2021.12.045
up_date	2024-07-06T23:58:02.686Z
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Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain

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