Literature DB >> 14998167

Identification of the chicken MARCKS phosphorylation site specific for differentiating neurons as Ser 25 using a monoclonal antibody and mass spectrometry.

Flavio R Zolessi1, Rosario Durán, Ulla Engström, Carlos Cerveñansky, Ulf Hellman, Cristina Arruti.   

Abstract

MARCKS is an actin-modulating protein that can be phosphorylated in multiple sites by PKC and proline-directed kinases. We have previously described a phosphorylated form of this protein specific for differentiating chick neurons, detected with mAb 3C3. Here, we show that this antibody binds to MARCKS only when it is phosphorylated at Ser 25. These and previous data provide hints for a possible answer to the question of why this ubiquitous protein seems to be essential only for neural development.

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Year:  2004        PMID: 14998167     DOI: 10.1021/pr034066f

Source DB:  PubMed          Journal:  J Proteome Res        ISSN: 1535-3893            Impact factor:   4.466


  3 in total

1.  Two myristoylated alanine-rich C-kinase substrate (MARCKS) paralogs are required for normal development in zebrafish.

Authors:  Laura E Ott; Zachary T McDowell; Poem M Turner; J McHugh Law; Kenneth B Adler; Jeffrey A Yoder; Samuel L Jones
Journal:  Anat Rec (Hoboken)       Date:  2011-08-01       Impact factor: 2.064

2.  A novel effect of MARCKS phosphorylation by activated PKC: the dephosphorylation of its serine 25 in chick neuroblasts.

Authors:  Andrea Toledo; Flavio R Zolessi; Cristina Arruti
Journal:  PLoS One       Date:  2013-04-25       Impact factor: 3.240

3.  Searching for novel Cdk5 substrates in brain by comparative phosphoproteomics of wild type and Cdk5-/- mice.

Authors:  Erick Contreras-Vallejos; Elías Utreras; Daniel A Bórquez; Michaela Prochazkova; Anita Terse; Howard Jaffe; Andrea Toledo; Cristina Arruti; Harish C Pant; Ashok B Kulkarni; Christian González-Billault
Journal:  PLoS One       Date:  2014-03-21       Impact factor: 3.240

  3 in total

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