BIP co-chaperone MTJ1/ERDJ1 interacts with inter-α-trypsin inhibitor heavy chain 4

Kroczyńska, Barbara; King-Simmons, LaShaunda; Alloza, Leonor; Álava, María Á.; Elguindi, Ebrahim C.; Blond, Sylvie Y.

doi:10.1016/j.bbrc.2005.10.101

Cited by 11 publications

(7 citation statements)

References 39 publications

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“…A first indication for a potential substrate specificity of ERj1 was reported by S. Y. Blond and coworkers (Kroczynska et al , 2004, 2005). In a two-hybrid screening these authors identified two interaction partners of the SANT-2 domain that is present in the cytosolic domain of human ERj1, the secretory proteins α1-antichymotrypsin (ACT, residues 140-400) and inter-α-trypsin inhibitor heavy chain 4 (ITIH4, residues 588-930).…”

Section: Discussionmentioning

confidence: 82%

Evolutionary Gain of Function for the ER Membrane Protein Sec62 from Yeast to Humans

Müller

Escauriaza

Lajoie

et al. 2010

MBoC

105

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Section: Discussionmentioning

confidence: 82%

Evolutionary Gain of Function for the ER Membrane Protein Sec62 from Yeast to Humans

Müller

Escauriaza

Lajoie

et al. 2010

MBoC

105

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“…This sequence is specific to ITIH4 isoform 1 and therefore contributes to isoform-specific glycosylation that may influence ITIH4 stability or interaction with the ECM. On the basis of expression studies, ITIH4 is primarily synthesized in the liver, and four isoforms of ITIH4 have been predicted based on mRNA and/or cDNA sequencing experiments. ,, Three ITIH4 isoforms have been described in adult liver tissue, while the fourth was found in fetal human liver. Isoform 1 was the first to be described and has been selected as the “canonical” sequence in UniProt.…”

Section: Discussionmentioning

confidence: 99%

Site-Specific Glycan Microheterogeneity of Inter-Alpha-Trypsin Inhibitor Heavy Chain H4

et al. 2014

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Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum. ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in liver disease. In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry. Recombinant ITIH4 was analyzed to optimize glycopeptide analyses, followed by serum-derived ITIH4. First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of 18O water. Next, we performed glycosidase-assisted LC–MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms. While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ. A fifth N-glycosylation site was discovered at N274 with the rare nonconsensus NVV motif. Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4. We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.

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“…Though some of them can bind misfolded polypeptides directly (e.g. ERdj3 [113] or MTJ1 [122]), others function without client binding, and yet others, like Sec63, are specific not for protein folding, but rather for translocation across the ER membrane. Considering the important role of the J domain proteins in regulating BiP’s ATPase cycle, deletions of two J proteins in the mouse have surprisingly specific phenotypes.…”

Section: Chaperone Network In the Ermentioning

confidence: 99%

Orchestration of secretory protein folding by ER chaperones

Gidalevitz

Stevens

Argon

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

121

115

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The endoplasmic reticulum is a major compartment of protein biogenesis in the cell, dedicated to production of secretory, membrane and organelle proteins. The secretome has distinct structural and post-translational characteristics, since folding in the ER occurs in an environment that is distinct in terms of its ionic composition, dynamics and requirements for quality contol. The folding machinery in the ER therefore includes chaperones and folding enzymes that introduce, monitor and react to disulfide bonds, glycans, and fluctuations of luminal calcium. We describe the major chaperone networks in the lumen and discuss how they have distinct modes of operation that enable cells to accomplish highly efficient production of the secretome.

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BIP co-chaperone MTJ1/ERDJ1 interacts with inter-α-trypsin inhibitor heavy chain 4

Cited by 11 publications

References 39 publications

Evolutionary Gain of Function for the ER Membrane Protein Sec62 from Yeast to Humans

Evolutionary Gain of Function for the ER Membrane Protein Sec62 from Yeast to Humans

Site-Specific Glycan Microheterogeneity of Inter-Alpha-Trypsin Inhibitor Heavy Chain H4

Orchestration of secretory protein folding by ER chaperones

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