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Wolverhampton Intellectual Repository and E-Theses > Research Institutes > Research Institute in Healthcare Science > Molecular Pharmacology Research Group > Intracellular translocation of the decapeptide carboxyl terminal of Gi3 alpha induces the dual phosphorylation of p42/p44 MAP kinases.

Please use this identifier to cite or link to this item: http://hdl.handle.net/2436/15802
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Title: Intracellular translocation of the decapeptide carboxyl terminal of Gi3 alpha induces the dual phosphorylation of p42/p44 MAP kinases.
Authors: Jones, Sarah
Farquhar, Michelle
Martin, Ashley
Howl, John D.
Citation: Biochimica Biophysica Acta - Molecular Cell Research, 1745(2): 207-214
Publisher: Elsevier BV
Issue Date: 2005
URI: http://hdl.handle.net/2436/15802
DOI: 10.1016/j.bbamcr.2005.05.006
PubMed ID: 15953648
Additional Links: http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T20-4G98WPV-2&_user=1644469&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000054077&_version=1&_urlVersion=0&_userid=1644469&md5=562f7956021f4bd397af6452096f9d8a
Abstract: The carboxyl terminal of heterotrimeric G protein alpha subunits binds both G protein-coupled receptors and mastoparan (MP), a tetradecapeptide allostere. Moreover, peptides corresponding to the carboxyl domains of G(i)3alpha and G(t) display intrinsic biological activities in cell-free systems. Thus, the purpose of this study was to develop a cell penetrant delivery system to further investigate the biological properties of a peptide mimetic of the G(i)3alpha carboxyl terminal (G(i)3alpha(346-355); H-KNNLKECGLY-NH2). Kinetic studies, using a CFDA-conjugated analogue of G(i)3alpha(346-355), confirmed the rapid and efficient intracellular translocation of TP10-G(i)3alpha(346-355) (t(0.5) = 3 min). Translocated G(i)3alpha(346-355), but not other bioactive cargoes derived from PKC and the CB1 cannabinoid receptor, promoted the dual phosphorylation of p42/p44 MAPK without adverse changes in cellular viability. The relative specificity of this novel biological activity was further confirmed by the observation that translocated G(i)3alpha(346-355) did not influence the exocytosis of beta-hexoseaminidase from RBL-2H3, a secretory event stimulated by other cell penetrant peptide cargoes and MP. We conclude that TP10-G(i)3alpha(346-355) is a valuable, non-toxic research tool with which to study and modulate signal transduction pathways mediated by heterotrimeric G proteins and MAPK.
Type: Article
Language: en
Description: Metadata only
Keywords: Mastoparan
Secretion
p42/p44 MAP kinase
G protein
Cell Penetrating Peptides (CPP)
Signalling
ISSN: 0006-3002
Appears in Collections: Molecular Pharmacology Research Group

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