Structural characterization of a neuroblast-specific phosphorylated region of MARCKS

Tinoco, Luzineide W.; Fraga, Jully Lacerda; Anobom, Cristiane D.; Zolessi, Flavio R.; Obal, Gonzalo; Toledo, Andrea; Pritsch, Otto; Arruti, Cristina

doi:10.1016/j.bbapap.2014.02.016

Cited by 8 publications

(5 citation statements)

References 47 publications

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“…MARCKS crosslinks actin filaments at the plasma membrane probably to facilitate morphological changes at the membrane and, in addition, has the ability to concentrate signaling molecules within membrane microdomains and interacts with adhesion molecules facilitating synapse, functions that are controlled by its effector domain regulated in phosphorylation dependent manner [41] . Phosphorylation on Ser26, detected in our data set, is specific in neurons but does not affect its association with membranes [42] . Given these characteristics, MARCKS could be explored as marker for SH-SY5Y differentiation.…”

Section: Resultsmentioning

confidence: 53%

Quantitative proteomic analysis identifies proteins and pathways related to neuronal development in differentiated SH-SY5Y neuroblastoma cells

Murillo

Goto‐Silva

Sánchez

et al. 2017

EuPA Open Proteomics

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Section: Resultsmentioning

confidence: 53%

Quantitative proteomic analysis identifies proteins and pathways related to neuronal development in differentiated SH-SY5Y neuroblastoma cells

Murillo

Goto‐Silva

Sánchez

et al. 2017

EuPA Open Proteomics

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“…Recently, the S25 residue within the relatively uncharacterized, but highly conserved, MARCKS MH2 domain was demonstrated to be phosphorylated by proline-directed kinases; primarily cdk5. This domain is only phosphorylated in neurons, does not affect association with membranes, and is yet to be functionally characterized (Tinoco et al, 2014 ). Interestingly, MARCKS has been demonstrated to cluster in groups with comparable phosphorylation states at the mutually exclusive S25 and ED residues (Toledo et al, 2013 ), perhaps due to the localization patterns induced by these modifications.…”

mentioning

confidence: 99%

X MARCKS the spot: myristoylated alanine-rich C kinase substrate in neuronal function and disease

Brudvig

Weimer

2015

Front. Cell. Neurosci.

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Intracellular protein-protein interactions are dynamic events requiring tightly regulated spatial and temporal checkpoints. But how are these spatial and temporal cues integrated to produce highly specific molecular response patterns? A helpful analogy to this process is that of a cellular map, one based on the fleeting localization and activity of various coordinating proteins that direct a wide array of interactions between key molecules. One such protein, myristoylated alanine-rich C-kinase substrate (MARCKS) has recently emerged as an important component of this cellular map, governing a wide variety of protein interactions in every cell type within the brain. In addition to its well-documented interactions with the actin cytoskeleton, MARCKS has been found to interact with a number of other proteins involved in processes ranging from intracellular signaling to process outgrowth. Here, we will explore these diverse interactions and their role in an array of brain-specific functions that have important implications for many neurological conditions.

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“…37 In addition, MARCKS is one of the most predominant substrates for protein kinase C (PKC) and can be phosphorylated by PKC or bind to calcium-calmodulin to inhibit its association with actin and the plasma membrane, leading to its presence in the cytoplasm. 38,39 Furthermore, one domain of MARCKS known as the phosphorylation site domain appears to play a key role in regulating MARCKS functions in its phosphorylated and dephosphorylated forms. 40 No obvious changes in MARCKS-S170 phosphorylation levels were observed 2-hour postinfection of HFF cells by T. gondii, whereas a large upregulation was found at 6-hour postinfection.…”

Section: Discussionmentioning

confidence: 99%

Phosphoproteome of Toxoplasma gondii Infected Host Cells Reveals Specific Cellular Processes Predominating in Different Phases of Infection

Chen

Wei

et al. 2017

The American Society of Tropical Medicine and Hygiene

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The invasion of tachyzoites into the host cell results in extensive host cell signaling activation/deactivation that is usually regulated by the phosphorylation/dephosphorylation. To elucidate how regulates host cell signal transduction, the comparative phosphoproteome of stable isotope labeling with amino acids in cell culture-labeled human foreskin fibroblast cells was analyzed. The cells were grouped (Light [L], Medium [M], and Heavy [H] groups) based on the labeling isotope weight and were infected with for different lengths of time (L: 0 hour; M: 2 hours; and H: 6 hours). A total of 892 phosphoproteins were identified with 1,872 phosphopeptides and 1,619 phosphorylation sites. The M versus L comparison revealed 694 significantly regulated phosphopeptides (436 upregulated and 258 downregulated). The H versus L comparison revealed 592 significantly regulated phosphopeptides (146 upregulated and 446 downregulated). The H versus M comparison revealed 794 significantly regulated phosphopeptides (149 upregulated and 645 downregulated). At 2 and 6 hours post- infection, the most predominant host cell reactions were cell cycle regulation and cytoskeletal reorganization, which might be required for the efficient invasion and multiplication of . Similar biological process profiles but different molecular function categories of host cells infected with for 2 and 6 hours, which suggested that the host cell processes were not affected significantly by infection but emphasized some differences in specific cellular processes at this two time points. Western blotting verification of some significantly regulated phosphoprotein phosphorylation sites was consistent with the mass spectra data. This study provided new insights into and further understanding of pathogen-host interactions from the host cell perspective.

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Structural characterization of a neuroblast-specific phosphorylated region of MARCKS

Cited by 8 publications

References 47 publications

Quantitative proteomic analysis identifies proteins and pathways related to neuronal development in differentiated SH-SY5Y neuroblastoma cells

Quantitative proteomic analysis identifies proteins and pathways related to neuronal development in differentiated SH-SY5Y neuroblastoma cells

X MARCKS the spot: myristoylated alanine-rich C kinase substrate in neuronal function and disease

Phosphoproteome of Toxoplasma gondii Infected Host Cells Reveals Specific Cellular Processes Predominating in Different Phases of Infection

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