MARCKS in Advanced Stages of Neural Retina Histogenesis

Zolessi, Flavio R.; Arruti, Cristina

doi:10.1159/000082279

Cited by 5 publications

(2 citation statements)

References 67 publications

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“…However, supporting a role for Marcksa and Marcksb in other aspects of neural development, we observed abnormal retinal histogenesis in MARCKS targeted zebrafish embryos (Fig. 7), and this data correlates with data that previously established MARCKS involvement in the histogenesis of the retina (Stumpo et al, 1995, Zolessi and Arruti, 2004). Specifically, it was found that the thick non‐nuclear layer (layer of Chievitz) was absent in MARCKS homozygous deficient mice retinas (Stumpo et al, 1995).…”

Section: Discussionsupporting

confidence: 91%

Two Myristoylated Alanine‐Rich C‐Kinase Substrate (MARCKS) Paralogs are Required for Normal Development in Zebrafish

Ott

Mcdowell

Turner

et al. 2011

The Anatomical Record

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Myristoylated alanine-rich C-kinase substrate (MARCKS) is an actin binding protein substrate of protein kinase C (PKC) and critical for mouse and Xenopus development. Herein two MARCKS paralogs, marcksa and marcksb, are identified in zebrafish and the role of these genes in zebrafish development is evaluated. Morpholino-based targeting of either MARCKS protein resulted in increased mortality and a range of gross phenotypic abnormalities. Phenotypic abnormalities were classified as mild, moderate or severe, which is characterized by a slight curve of a full-length tail, a severe curve or twist of a full-length tail and a truncated tail, respectively. All three phenotypes displayed abnormal neural architecture. Histopathology of Marcks targeted embryos revealed abnormalities in retinal layering, gill formation and skeletal muscle morphology. These results demonstrate that Marcksa and Marcksb are required for normal zebrafish development and suggest that zebrafish are a suitable model to further study MARCKS function.

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Section: Discussionsupporting

confidence: 91%

Two Myristoylated Alanine‐Rich C‐Kinase Substrate (MARCKS) Paralogs are Required for Normal Development in Zebrafish

Ott

Mcdowell

Turner

et al. 2011

The Anatomical Record

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“…It only exhibited slight differences in intensity along the retinal plane, in correlation with the central to peripheral differentiation gradient (as it was already described [28]). pED-MARCKS was nearly completely absent, only detectable in some mitotic cells and in neuroblasts located close to the vitreal surface of the neural retina (Fig.…”

Section: Resultssupporting

confidence: 71%

A Novel Effect of MARCKS Phosphorylation by Activated PKC: The Dephosphorylation of Its Serine 25 in Chick Neuroblasts

2013

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MARCKS (Myristoylated Alanine-Rich C Kinase Substrate) is a peripheral membrane protein, especially abundant in the nervous system, and functionally related to actin organization and Ca-calmodulin regulation depending on its phosphorylation by PKC. However, MARCKS is susceptible to be phosphorylated by several different kinases and the possible interactions between these phosphorylations have not been fully studied in intact cells. In differentiating neuroblasts, as well as some neurons, there is at least one cell-type specific phosphorylation site: serine 25 (S25) in the chick. We demonstrate here that S25 is included in a highly conserved protein sequence which is a Cdk phosphorylatable region, located far away from the PKC phosphorylation domain. S25 phosphorylation was inhibited by olomoucine and roscovitine in neuroblasts undergoing various states of cell differentiation in vitro. These results, considered in the known context of Cdks activity in neuroblasts, suggest that Cdk5 is the enzyme responsible for this phosphorylation. We find that the phosphorylation by PKC at the effector domain does not occur in the same molecules that are phosphorylated at serine 25. The in situ analysis of the subcellular distribution of these two phosphorylated MARCKS variants revealed that they are also segregated in different protein clusters. In addition, we find that a sustained stimulation of PKC by phorbol-12-myristate-13-acetate (PMA) provokes the progressive disappearance of phosphorylation at serine 25. Cells treated with PMA, but in the presence of several Ser/Thr phosphatase (PP1, PP2A and PP2B) inhibitors indicated that this dephosphorylation is achieved via a phosphatase 2A (PP2A) form. These results provide new evidence regarding the existence of a novel consequence of PKC stimulation upon the phosphorylated state of MARCKS in neural cells, and propose a link between PKC and PP2A activity on MARCKS.

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Structural characterization of a neuroblast-specific phosphorylated region of MARCKS

Tinoco

Fraga

Anobom

et al. 2014

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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MARCKS in Advanced Stages of Neural Retina Histogenesis

Cited by 5 publications

References 67 publications

Two Myristoylated Alanine‐Rich C‐Kinase Substrate (MARCKS) Paralogs are Required for Normal Development in Zebrafish

Two Myristoylated Alanine‐Rich C‐Kinase Substrate (MARCKS) Paralogs are Required for Normal Development in Zebrafish

A Novel Effect of MARCKS Phosphorylation by Activated PKC: The Dephosphorylation of Its Serine 25 in Chick Neuroblasts

Structural characterization of a neuroblast-specific phosphorylated region of MARCKS

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