Mapping the Ca2+ induced structural change in calreticulin
Calreticulin is a highly conserved multifunctional protein implicated in many different biological systems and has therefore been the subject of intensive research. It is primarily present in the endoplasmatic reticulum where its main functions are to regulate Ca2+ homeostasis, act as a chaperone an...
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| Published in | Journal of proteomics Vol. 142; pp. 138 - 148 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
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Elsevier B.V
16.06.2016
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| Subjects | |
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| Abstract | Calreticulin is a highly conserved multifunctional protein implicated in many different biological systems and has therefore been the subject of intensive research. It is primarily present in the endoplasmatic reticulum where its main functions are to regulate Ca2+ homeostasis, act as a chaperone and stabilize the MHC class I peptide-loading complex. Although several high-resolution structures of calreticulin exist, these only cover three-quarters of the entire protein leaving the extended structures unsolved. Additionally, the structure of calreticulin is influenced by the presence of Ca2+. The conformational changes induced by Ca2+ have not been determined yet as they are hard to study with traditional approaches. Here, we investigated the Ca2+-induced conformational changes with a combination of chemical cross-linking, mass spectrometry, bioinformatics analysis and modelling in Rosetta. Using a bifunctional linker, we found a large Ca2+-induced change to the cross-linking pattern in calreticulin. Our results are consistent with a high flexibility in the P-loop, a stabilization of the acidic C-terminal and a relatively close interaction of the P-loop and the acidic C-terminal.
The function of calreticulin, an endoplasmatic reticulin chaperone, is affected by fluctuations in Ca2+concentration, but the structural mechanism is unknown. The present work suggests that Ca2+-dependent regulation is caused by different conformations of a long proline-rich loop that changes the accessibility to the peptide/lectin-binding site. Our results indicate that the binding of Ca2+ to calreticulin may thus not only just be a question of Ca2+ storage but is likely to have an impact on the chaperone activity.
[Display omitted]
•Conformational changes of calreticulin can be monitored by cross-linking and MS.•The location of the P-loop is dependent on the concentration of Ca2+.•Part of the disordered acidic C-terminal is stabilized by Ca2+. |
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| AbstractList | Calreticulin is a highly conserved multifunctional protein implicated in many different biological systems and has therefore been the subject of intensive research. It is primarily present in the endoplasmatic reticulum where its main functions are to regulate Ca2 + homeostasis, act as a chaperone and stabilize the MHC class I peptide-loading complex. Although several high-resolution structures of calreticulin exist, these only cover three-quarters of the entire protein leaving the extended structures unsolved. Additionally, the structure of calreticulin is influenced by the presence of Ca2 +. The conformational changes induced by Ca2 + have not been determined yet as they are hard to study with traditional approaches. Here, we investigated the Ca2 +-induced conformational changes with a combination of chemical cross-linking, mass spectrometry, bioinformatics analysis and modelling in Rosetta. Using a bifunctional linker, we found a large Ca2 +-induced change to the cross-linking pattern in calreticulin. Our results are consistent with a high flexibility in the P-loop, a stabilization of the acidic C-terminal and a relatively close interaction of the P-loop and the acidic C-terminal. Biological significance The function of calreticulin, an endoplasmatic reticulin chaperone, is affected by fluctuations in Ca2 + concentration, but the structural mechanism is unknown. The present work suggests that Ca2 +-dependent regulation is caused by different conformations of a long proline-rich loop that changes the accessibility to the peptide/lectin-binding site. Our results indicate that the binding of Ca2 + to calreticulin may thus not only just be a question of Ca2 + storage but is likely to have an impact on the chaperone activity. Calreticulin is a highly conserved multifunctional protein implicated in many different biological systems and has therefore been the subject of intensive research. It is primarily present in the endoplasmatic reticulum where its main functions are to regulate Ca2 + homeostasis, act as a chaperone and stabilize the MHC class I peptide-loading complex. Although several high-resolution structures of calreticulin exist, these only cover three-quarters of the entire protein leaving the extended structures unsolved. Additionally, the structure of calreticulin is influenced by the presence of Ca2 +. The conformational changes induced by Ca2 + have not been determined yet as they are hard to study with traditional approaches. Here, we investigated the Ca2 +-induced conformational changes with a combination of chemical cross-linking, mass spectrometry, bioinformatics analysis and modelling in Rosetta. Using a bifunctional linker, we found a large Ca2 +-induced change to the cross-linking pattern in calreticulin. Our results are consistent with a high flexibility in the P-loop, a stabilization of the acidic C-terminal and a relatively close interaction of the P-loop and the acidic C-terminal. Biological significance The function of calreticulin, an endoplasmatic reticulin chaperone, is affected by fluctuations in Ca2 + concentration, but the structural mechanism is unknown. The present work suggests that Ca2 +-dependent regulation is caused by different conformations of a long proline-rich loop that changes the accessibility to the peptide/lectin-binding site. Our results indicate that the binding of Ca2 + to calreticulin may thus not only just be a question of Ca2 + storage but is likely to have an impact on the chaperone activity. Calreticulin is a highly conserved multifunctional protein implicated in many different biological systems and has therefore been the subject of intensive research. It is primarily present in the endoplasmatic reticulum where its main functions are to regulate Ca2+ homeostasis, act as a chaperone and stabilize the MHC class I peptide-loading complex. Although several high-resolution structures of calreticulin exist, these only cover three-quarters of the entire protein leaving the extended structures unsolved. Additionally, the structure of calreticulin is influenced by the presence of Ca2+. The conformational changes induced by Ca2+ have not been determined yet as they are hard to study with traditional approaches. Here, we investigated the Ca2+-induced conformational changes with a combination of chemical cross-linking, mass spectrometry, bioinformatics analysis and modelling in Rosetta. Using a bifunctional linker, we found a large Ca2+-induced change to the cross-linking pattern in calreticulin. Our results are consistent with a high flexibility in the P-loop, a stabilization of the acidic C-terminal and a relatively close interaction of the P-loop and the acidic C-terminal. The function of calreticulin, an endoplasmatic reticulin chaperone, is affected by fluctuations in Ca2+concentration, but the structural mechanism is unknown. The present work suggests that Ca2+-dependent regulation is caused by different conformations of a long proline-rich loop that changes the accessibility to the peptide/lectin-binding site. Our results indicate that the binding of Ca2+ to calreticulin may thus not only just be a question of Ca2+ storage but is likely to have an impact on the chaperone activity. [Display omitted] •Conformational changes of calreticulin can be monitored by cross-linking and MS.•The location of the P-loop is dependent on the concentration of Ca2+.•Part of the disordered acidic C-terminal is stabilized by Ca2+. Calreticulin is a highly conserved multifunctional protein implicated in many different biological systems and has therefore been the subject of intensive research. It is primarily present in the endoplasmatic reticulum where its main functions are to regulate Ca²⁺ homeostasis, act as a chaperone and stabilize the MHC class I peptide-loading complex. Although several high-resolution structures of calreticulin exist, these only cover three-quarters of the entire protein leaving the extended structures unsolved. Additionally, the structure of calreticulin is influenced by the presence of Ca²⁺. The conformational changes induced by Ca²⁺ have not been determined yet as they are hard to study with traditional approaches. Here, we investigated the Ca²⁺-induced conformational changes with a combination of chemical cross-linking, mass spectrometry, bioinformatics analysis and modelling in Rosetta. Using a bifunctional linker, we found a large Ca²⁺-induced change to the cross-linking pattern in calreticulin. Our results are consistent with a high flexibility in the P-loop, a stabilization of the acidic C-terminal and a relatively close interaction of the P-loop and the acidic C-terminal.The function of calreticulin, an endoplasmatic reticulin chaperone, is affected by fluctuations in Ca²⁺concentration, but the structural mechanism is unknown. The present work suggests that Ca²⁺-dependent regulation is caused by different conformations of a long proline-rich loop that changes the accessibility to the peptide/lectin-binding site. Our results indicate that the binding of Ca²⁺ to calreticulin may thus not only just be a question of Ca²⁺ storage but is likely to have an impact on the chaperone activity. |
| Author | Boelt, Sanne Grundvad Čiplys, Evaldas Slibinskas, Rimantas Højrup, Peter Norn, Christoffer Houen, Gunnar Rasmussen, Morten Ib André, Ingemar |
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| Snippet | Calreticulin is a highly conserved multifunctional protein implicated in many different biological systems and has therefore been the subject of intensive... |
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| SubjectTerms | bioinformatics Biologi Biological Sciences BS d BS3 d0 BS3 d4 calcium Calreticulin Chemical cross-linking crosslinking endoplasmic reticulum homeostasis Mass spectrometry MassAI software Natural Sciences Naturvetenskap Protein structure reticulin Rosetta modelling |
| Title | Mapping the Ca2+ induced structural change in calreticulin |
| URI | https://dx.doi.org/10.1016/j.jprot.2016.05.015 https://www.proquest.com/docview/1825426478 https://lup.lub.lu.se/record/c33c8e43-a5ea-4c46-881b-15241d4ebd61 oai:portal.research.lu.se:publications/c33c8e43-a5ea-4c46-881b-15241d4ebd61 |
| Volume | 142 |
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