Phosphorylation of serine 4642 in the C-terminus of plectin by MNK2 and PKA modulates its interaction with intermediate filaments

Journal of Cell Science

Volumn 126, Issue 18, 2013, Pages 4195-4207

  Bouameur, Jamal Eddine ^a   Schneider, Yann ^b   Begre, Nadja ^a   Hobbs, Ryan P ^c   Lingasamy, Prakash ^a   Fontao, Lionel ^b   Green, Kathleen J ^c   Favre, Bertrand ^a   Borradori, Luca ^a  

^a UNIVERSITY OF BERN   (Switzerland)

^b GENEVA UNIVERSITY HOSPITALS   (Switzerland)

^c NORTHWESTERN UNIVERSITY   (United States)

Author keywords

Cytoskeleton; Intermediate filaments; Plakin; Plectin; Protein phosphorylation

Indexed keywords

8 BROMO CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; EPIDERMAL GROWTH FACTOR; INTERMEDIATE FILAMENT BINDING DOMAIN PROTEIN; INTERMEDIATE FILAMENT PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE INTERACTING KINASE 2; PHORBOL ESTER; PHOSPHOPROTEIN PHOSPHATASE 2A; PLECTIN; PROTEIN KINASE INHIBITOR; PROTEINASE; SERINE; SORBITOL; UNCLASSIFIED DRUG; MKNK2 PROTEIN, HUMAN; PLAKIN; PROTEIN SERINE THREONINE KINASE; SIGNAL PEPTIDE;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL CULTURE; CELL FRACTIONATION; CONTROLLED STUDY; CYTOSKELETON; FEMALE; HELA CELL; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE MICROSCOPY; INTERMEDIATE FILAMENT; KERATINOCYTE; MEDIATOR; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SKIN; TUMOR CELL LINE; WOUND HEALING; YEAST; CELL MOTION; GENETIC TRANSFECTION; GENETICS; METABOLISM; PHOSPHORYLATION; PROTEIN BINDING;

CYTOSKELETON; INTERMEDIATE FILAMENTS; PLAKIN; PLECTIN; PROTEIN PHOSPHORYLATION;

CELL MOVEMENT; CYTOSKELETON; HUMANS; INTERMEDIATE FILAMENTS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; PHOSPHORYLATION; PLECTIN; PROTEIN BINDING; PROTEIN-SERINE-THREONINE KINASES; SERINE; TRANSFECTION;

EID: 84885440077     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.127779     Document Type: Article

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