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

Glading, A.; Bodnar, R. J.; Reynolds, I. J.; Shiraha, H.; Satish, L.; Potter, D. A.; Blair, H. C.; Wells, A.

doi:10.1128/mcb.24.6.2499-2512.2004

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

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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EGFR-mediated activation of epithelial proteases, particularly m-calpain through MAPK activity, contributed substantially to bacterial invasion across the tight junctions of the airway epithelium, demonstrated both in vitro and in vivo.
“EGFR-mediated activation of epithelial proteases, particularly m-calpain through MAPK activity, contributed substantially to bacterial invasion across the tight junctions of the airway epithelium (27), demonstrated both in vitro and in vivo.”
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Membrane Proximal ERK Signaling Is Required for M-calpain Activation Downstream of Epidermal Growth Factor Receptor Signaling
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Epidermal growth factor activates m-calpain, resulting in apoptosis of HaCaT keratinocytes
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Spatial Localization of m-Calpain to the Plasma Membrane by Phosphoinositide Biphosphate Binding during Epidermal Growth Factor Receptor-Mediated Activation
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Activation of m-Calpain (Calpain II) by Epidermal Growth Factor Is Limited by Protein Kinase A Phosphorylation of m-Calpain
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Self-citation

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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