The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Functional specialization of calreticulin domains
Open accessAbstract
Calreticulin is a Ca2+-binding chaperone in the endoplasmic reticulum (ER), and calreticulin gene knockout is embryonic lethal. Here, we used calreticulin-deficient mouse embryonic fibroblasts to examine the function of calreticulin as a regulator of Ca2+ homeostasis. In cells without calreticulin, the ER has a lower capacity for Ca2+ storage, although the free ER luminal Ca2+ concentration is unchanged. Calreticulin-deficient cells show inhibited Ca2+ release in response to bradykinin, yet they release Ca2+ upon direct activation with the inositol 1,4,5-trisphosphate (InsP3). These cells fail to produce a measurable level of InsP3 upon stimulation with bradykinin, likely because the binding of bradykinin to its cell surface receptor is impaired. Bradykinin binding and bradykinin-induced Ca2+ release are both restored by expression of full-length calreticulin and the N + P domain of the protein. Expression of the P + C domain of calreticulin does not affect bradykinin-induced Ca2+ release but restores the ER Ca2+ storage capacity. Our results indicate that calreticulin may play a role in folding of the bradykinin receptor, which affects its ability to initiate InsP3-dependent Ca2+ release in calreticulin-deficient cells. We concluded that the C domain of calreticulin plays a role in Ca2+ storage and that the N domain may participate in its chaperone functions.
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Cites
Fluorescent indicators for Ca2+based on green fluorescent proteins and calmodulin
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Self-citationA Practical Guide to the Preparation of Ca2+ Buffers
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Calnexin: a membrane-bound chaperone of the endoplasmic reticulum
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Calreticulin Is Essential for Cardiac Development
Mesaeli, N., Nakamura, K., Zvaritch, E., Dickie, P., Dziak, E., Krause, K.-H., Opas, M., MacLennan, D. H., & Michalak, M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.5.857 · Cited by 514
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Cited by
ER chaperone functions during normal and stress conditions
Ma, Y., & Hendershot, L. M. (2004) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2003.08.007 · Cited by 440
Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum
Gelebart, P., Opas, M., & Michalak, M. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.030 · Cited by 261
Self-citationYáñez, M., Gil-Longo, J., & Campos-Toimil, M. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-94-007-2888-2_19 · Cited by 195
Zarate, S. M., Huntington, T. E., Bagher, P., & Srinivasan, R. (2023) · npj Aging · doi:10.1038/s41514-023-00102-8 · Cited by 19
Metadata
- Authors
- Nakamura, K., Zuppini, A., Arnaudeau, S., Lynch, J., Ahsan, I., Krause, R., Papp, S., De Smedt, H., Parys, J. B., Müller-Esterl, W., Lew, D. P., Krause, K.-H., Demaurex, N., Opas, M., & Michalak, M.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2001-08-27
- Volume
- 154
- Issue
- 5
- Pages
- 961-972
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2135913162
- Cited by
- 317
- References
- 31
- FWCI
- 4.52
- Type
- journal article
- Language
- en
- Open access
- green
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- Nakamura, K., Zuppini, A., Arnaudeau, S., Lynch, J., Ahsan, I., Krause, R., Papp, S., De Smedt, H., Parys, J. B., Müller-Esterl, W., Lew, D. P., Krause, K.-H., Demaurex, N., Opas, M., & Michalak, M. (2001). Functional specialization of calreticulin domains. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200102073
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