Literature DB >> 15855766

MARCKS in advanced stages of neural retina histogenesis.

Flavio R Zolessi1, Cristina Arruti.   

Abstract

Myristoylated alanine-rich kinase C substrate (MARCKS), an actin-binding protein, is involved in several signal transduction pathways. It is susceptible to be phosphorylated by protein kinases as protein kinase C and some proline-directed kinases. These phosphorylations differently modulate its functions. We previously showed that a phosphorylation at its Ser25 (S25p-MARCKS) in chickens is a signature of this ubiquitous protein in neuron differentiation. To gain insight into the possible involvement of MARCKS in late retinal histogenesis, we compared the developmental expression patterns of the total protein and its S25p variants. Here we show that the most outstanding modifications occur at the outer retina, where S25p disappears at the end of embryonic development and where MARCKS is missing in adults. These results suggest diverse functional specializations in the different retinal layers. Copyright 2004 S. Karger AG, Basel.

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Year:  2004        PMID: 15855766     DOI: 10.1159/000082279

Source DB:  PubMed          Journal:  Dev Neurosci        ISSN: 0378-5866            Impact factor:   2.984


  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.  Identification of HMX1 target genes: a predictive promoter model approach.

Authors:  Arnaud Boulling; Linda Wicht; Daniel F Schorderet
Journal:  Mol Vis       Date:  2013-08-06       Impact factor: 2.367

  3 in total

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