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Volumn 20, Issue 5, 2008, Pages 589-596

Regulation of hemidesmosome disassembly by growth factor receptors

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH FACTOR RECEPTOR; TYROSINE;

EID: 50849108513     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2008.05.001     Document Type: Review
Times cited : (88)

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    • Rabinovitz, I.1    Tsomo, L.2    Mercurio, A.M.3
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    • 34548477663 scopus 로고    scopus 로고
    • Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor-induced hemidesmosome disruption
    • This is an elegant work demonstrating serines 1356, 1360, 1364 as important phosphorylation sites involved in EGF-induced HD disassembly in human keratinocytes. S1360 and S1364 were identified as sites for PKC and PKA, respectively. Using mutants carrying aspartic acid or alanine substitutions, it was shown that the phosphorylation of two or more of the serines prevents binding of the plectin ABD to β4. Whereas triple aspartic acid mutations prevented HD assembly, substitution to the same residues to alanines provided partial protection against EGF-induced HD disassembly.
    • Wilhelmsen K., Litjens S.H.M., Kuikman I., Margadant C., van Rheenen J., and Sonnenberg A. Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor-induced hemidesmosome disruption. Mol Biol Cell 18 (2007) 3512-3522. This is an elegant work demonstrating serines 1356, 1360, 1364 as important phosphorylation sites involved in EGF-induced HD disassembly in human keratinocytes. S1360 and S1364 were identified as sites for PKC and PKA, respectively. Using mutants carrying aspartic acid or alanine substitutions, it was shown that the phosphorylation of two or more of the serines prevents binding of the plectin ABD to β4. Whereas triple aspartic acid mutations prevented HD assembly, substitution to the same residues to alanines provided partial protection against EGF-induced HD disassembly.
    • (2007) Mol Biol Cell , vol.18 , pp. 3512-3522
    • Wilhelmsen, K.1    Litjens, S.H.M.2    Kuikman, I.3    Margadant, C.4    van Rheenen, J.5    Sonnenberg, A.6
  • 49
    • 27644496163 scopus 로고    scopus 로고
    • Mobilization and activation of a signaling competent α6β4 integrin underlies its contribution to carcinoma progression
    • Lipscomb E.A., and Mercurio A.M. Mobilization and activation of a signaling competent α6β4 integrin underlies its contribution to carcinoma progression. Cancer Metastasis Rev 24 (2005) 413-423
    • (2005) Cancer Metastasis Rev , vol.24 , pp. 413-423
    • Lipscomb, E.A.1    Mercurio, A.M.2
  • 50
    • 21744455891 scopus 로고    scopus 로고
    • Targeted deletion of the integrin β4 cytoplasmic domain suppresses laminin-5 dependent nuclear entry of mitogen activated protein kinases and NF-κB, causing defects in epidermal growth and migration
    • In this study, mice were generated carrying a targeted deletion of the cytoplasmic domain of β4 downstream of residue 1355. Despite epidermal hypoplasia and reduced wound healing, HD formation and stable adhesion to the BM in these mice were not impaired, demonstrating that the part upstream of residue 1355 that interacts with plectin is sufficient for HD assembly, whereas the downstream segment containing the serines and tyrosine described in the literature is not essential.
    • Nikolopoulos S.N., Blaikie P., Yoshioka T., Guo W., Puri C., Tacchetti C., and Giancotti F.G. Targeted deletion of the integrin β4 cytoplasmic domain suppresses laminin-5 dependent nuclear entry of mitogen activated protein kinases and NF-κB, causing defects in epidermal growth and migration. Mol Cell Biol 25 (2005) 6090-6102. In this study, mice were generated carrying a targeted deletion of the cytoplasmic domain of β4 downstream of residue 1355. Despite epidermal hypoplasia and reduced wound healing, HD formation and stable adhesion to the BM in these mice were not impaired, demonstrating that the part upstream of residue 1355 that interacts with plectin is sufficient for HD assembly, whereas the downstream segment containing the serines and tyrosine described in the literature is not essential.
    • (2005) Mol Cell Biol , vol.25 , pp. 6090-6102
    • Nikolopoulos, S.N.1    Blaikie, P.2    Yoshioka, T.3    Guo, W.4    Puri, C.5    Tacchetti, C.6    Giancotti, F.G.7
  • 51
    • 0032857374 scopus 로고    scopus 로고
    • Transmembrane signaling for adhesive regulation of desmosomes and hemidesmosomes, and for cell-cell detachment induced by pemphigus IgG in cultures keratinocytes: involvement of protein kinase C
    • Kitajima Y., Aoyama Y., and Seishima M. Transmembrane signaling for adhesive regulation of desmosomes and hemidesmosomes, and for cell-cell detachment induced by pemphigus IgG in cultures keratinocytes: involvement of protein kinase C. J Investig Dermatol Symp Proc 4 (1999) 137-144
    • (1999) J Investig Dermatol Symp Proc , vol.4 , pp. 137-144
    • Kitajima, Y.1    Aoyama, Y.2    Seishima, M.3
  • 52
    • 0042679580 scopus 로고    scopus 로고
    • The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration
    • A very interesting report demonstrating that stimulation of human keratinocytes with the Ron ligand MSP induces serine phosphorylation of both β4 and Ron at specific 14-3-3-binding sites, resulting in the 14-3-3-dependent formation of a Ron-α6β4 complex that result in the translocation of α6β4 from HDs to lamellipodia. This report thus emphasizes the importance of serine phosphorylations on integrin α6β4 in response to a physiological stimulus that induces HD disassembly and wound healing. In addition, it provides potential mechanism for serine phosphorylation-mediated HD disruption.
    • Santoro M.M., Gaudino G., and Marchisio P.C. The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration. Dev Cell 5 (2003) 257-271. A very interesting report demonstrating that stimulation of human keratinocytes with the Ron ligand MSP induces serine phosphorylation of both β4 and Ron at specific 14-3-3-binding sites, resulting in the 14-3-3-dependent formation of a Ron-α6β4 complex that result in the translocation of α6β4 from HDs to lamellipodia. This report thus emphasizes the importance of serine phosphorylations on integrin α6β4 in response to a physiological stimulus that induces HD disassembly and wound healing. In addition, it provides potential mechanism for serine phosphorylation-mediated HD disruption.
    • (2003) Dev Cell , vol.5 , pp. 257-271
    • Santoro, M.M.1    Gaudino, G.2    Marchisio, P.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.