Cited by 271Calpain Protease Function and RegulationProtein Kinase Regulation and GTPase SignalingS100 Proteins and Annexins

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Epidermal Growth Factor Activates m-Calpain (Calpain II), at Least in Part, by Extracellular Signal-Regulated Kinase-Mediated Phosphorylation

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Glading, A., Bodnar, R. J., Reynolds, I. J., Shiraha, H., Satish, L., Potter, D. A., Blair, H. C., Wells, A.·2004·Molecular and Cellular Biology

DOI 10.1128/mcb.24.6.2499-2512.2004PMC PMC355832

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Abstract

How m-calpain is activated in cells has challenged investigators because in vitro activation requires near-millimolar calcium. Previously, we demonstrated that m-calpain activation by growth factors requires extracellular signal-regulated kinase (ERK); this enables tail deadhesion and allows productive motility. We now show that ERK directly phosphorylates and activates m-calpain both in vitro and in vivo. We identified serine 50 as required for epidermal growth factor (EGF)-induced calpain activation in vitro and in vivo. Replacing the serine with alanine limits activation by EGF and subsequent cell deadhesion and motility. A construct with the serine converted to glutamic acid displays constitutive activity in vivo; expression of an estrogen receptor fusion construct produces a tamoxifen-sensitive enzyme. Interestingly, EGF-induced m-calpain activation occurs in the absence of increased intracellular calcium levels; EGF triggers calpain even in the presence of intracellular calcium chelators and in calcium-free media. These data provide evidence that m-calpain can be activated through the ERK cascade via direct phosphorylation and that this activation may occur in the absence of cytosolic calcium fluxes.

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A new generation of Ca2+ indicators with greatly improved fluorescence properties.
Grynkiewicz, G., Poenie, M., & Tsien, R. Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83641-4 · Cited by 21,562
Calcium-activated neutral protease (calpain) system: structure, function, and regulation.
Croall, D. E., & Demartino, G. (1991) · Physiological Reviews · doi:10.1152/physrev.1991.71.3.813 · Cited by 837
A modified oestrogen receptor ligand-binding domain as an improved switch for the regulation of heterologous proteins
Littlewood, T. D., Hancock, D. C., Danielian, P. S., Parker, M. G., & Evan, G. I. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.10.1686 · Cited by 782
Structure and physiological function of calpains
Sorimachi, H., Ishiura, S., & Suzuki, K. (1997) · Biochemical Journal · doi:10.1042/bj3280721 · Cited by 706
Spatiotemporal Dynamics of Inositol 1,4,5-Trisphosphate That Underlies Complex Ca 2+ Mobilization Patterns
Hirose, K., Kadowaki, S., Tanabe, M., Takeshima, H., & Iino, M. (1999) · Science · doi:10.1126/science.284.5419.1527 · Cited by 512
The organisation and functions of local Ca2+ signals
Bootman, M. D., Lipp, P., & Berridge, M. J. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.12.2213 · Cited by 449
Regulation of Cell Migration by the Calcium-dependent Protease Calpain
Huttenlocher, A., Palecek, S. P., Lu, Q., Zhang, W., Mellgren, R. L., Lauffenburger, D. A., Ginsberg, M. H., & Horwitz, A. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32719 · Cited by 390 · cited 2×
“Even whether calpains are activated at the cell front during spreading or at the rear during detachment has only been addressed indirectly (3, 26, 41, 43, 45).”
Background
Cutting to the chase: calpain proteases in cell motility
Glading, A., Lauffenburger, D. A., & Wells, A. H. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02179-1 · Cited by 388
Self-citation
The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium
Strobl, S., Fernandez-Catalan, C., Braun, M., Huber, R., Masumoto, H., Nakagawa, K., Irie, A., Sorimachi, H., Bourenkov, G. P., Bartunik, H. D., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.588 · Cited by 366
Crystal structure of calpain reveals the structural basis for Ca2+‐dependent protease activity and a novel mode of enzyme activation
Hosfield, C. M., Elce, J. S., Davies, P. L., & Jia, Z. (1999) · The EMBO Journal · doi:10.1093/emboj/18.24.6880 · Cited by 360

Show all 55 references

Research works printed but not linked: 2

Guttmann R. P., 2000, Methods Mol. Biol., 144, 143
Shiraha H., 1999, J. Cell Biol., 146, 243

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Authors: Glading, A., Bodnar, R. J., Reynolds, I. J., Shiraha, H., Satish, L., Potter, D. A., Blair, H. C., & Wells, A.
Affiliations: Departments of Pathology
Pharmacology
Indiana University School of Medicine (US)
University of Pittsburgh (US)
Veterans Health Administration (US)
Corresponding author: Wells, A.
ORCID: Glading, A.
Bodnar, R. J.
Reynolds, I. J.
Shiraha, H.
Satish, L.
Potter, D. A.
Blair, H. C.
Wells, A.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2004-03-01
Volume: 24
Issue: 6
Pages: 2499-2512
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.24.6.2499-2512.2004
PMC: PMC355832
OpenAlex: W2153992286
Cited by: 271
References: 55
Citations by year: 2026: 3 · 2025: 4 · 2024: 6 · 2023: 7 · 2022: 7 · 2021: 8 · 2020: 6 · 2019: 6 · 2018: 5 · 2017: 10 · 2016: 11 · 2015: 9 · 2014: 11 · 2013: 16 · 2012: 15
FWCI: 9.68
Type: journal article
Language: en
Update notices: correction (2004-07-01)
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Veterans Affairs
National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
Keywords: m-calpain, epidermal growth factor, ERK signaling, protein phosphorylation, calpain activation, cell motility, calcium-independent activation
MeSH terms: Animals, Base Sequence, Binding Sites, Calcium, Calpain, Cell Line, Cell Movement, Enzyme Activation, Epidermal Growth Factor, Humans, Phosphorylation, Recombinant Proteins, Serine, Mutagenesis, Site-Directed, DNA, Complementary, Amino Acid Substitution, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System, Mice, In Vitro Techniques

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Epidermal Growth Factor Activates m-Calpain (Calpain II), at Least in Part, by Extracellular Signal-Regulated Kinase-Mediated Phosphorylation

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