Matrin 3 is a Ca2+/calmodulin-binding protein cleaved by caspases

Valencia, C. Alexander; Ju, Wujian; Liu, Rihe

doi:10.1016/j.bbrc.2007.06.156

Cited by 30 publications

(12 citation statements)

References 19 publications

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“…Significantly, it was found that many of the mapped cleavage sites are located within or close to a structural domain, suggesting that the functions of these substrates could be altered or abolished by caspase-mediated proteolysis. In general, the mapped cleavage sites are consistent with the assigned classes reported in the literature [52]. In the case of caspase-3 substrates, P1 (amino acid that is C-terminally cleaved, additional sites are N-terminal from P1 labeled as P2, P3, etc.)…”

Section: Selection Results and Discussionsupporting

confidence: 87%

In vitro selection of proteins with desired characteristics using mRNA-display

Valencia

Zou

Liu

2013

Methods

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mRNA-display is an amplification-based, iterative rounds of in vitro protein selection technique that circumvents a number of difficulties associated with yeast two-hybrid and phage display. Because of the covalent linkage between the genotype and the phenotype, mRNA-display provides a powerful means for reading and amplifying a peptide or protein sequence after it has been selected from a library with very high diversity. The purpose of this article is to provide a summary of the field and practical framework of mRNA-display-based selections. We summarize the advantages and limitations of selections using mRNA-display as well as the recent applications, namely, the identification of novel affinity reagents, target-binding partners, and enzyme substrates from synthetic peptide or natural proteome libraries. Practically, we provide a detailed procedure for performing mRNA-display-based selections with the aim of identifying protease substrates and binding partners of a target protein. Furthermore, we describe how to confirm the function of the selected protein sequences by biochemical assays and bioinformatic tools.

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Section: Selection Results and Discussionsupporting

confidence: 87%

In vitro selection of proteins with desired characteristics using mRNA-display

Valencia

Zou

Liu

2013

Methods

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“…Moreover, alsin is also found to play a role in AMPAR trafficking, where ALS2 mutations lead to distinct subcellular GRIP1 localization and reduction of the calcium-impermeable GluR2 containing AMPA receptors, thus likely rendering neurons susceptible to deviant Ca 2+ influxes (Lai et al, 2006). Matrin 3, a multifunctional nuclear matrix protein involved in ALS21, is suggested to be regulated through a Ca 2+ dependent interaction with CaM (Valencia et al, 2007) and is therefore likely to be affected by deregulated Ca 2+ levels. As only very recently matrin 3 has been implicated in ALS (Johnson et al, 2014), future studies will be needed to clarify this possibility.…”

Section: Crossways Of Als Critical Proteins With Calciummentioning

confidence: 99%

Calcium dysregulation links ALS defective proteins and motor neuron selective vulnerability

Leal

Gomes

2015

Front. Cell. Neurosci.

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More than 20 distinct gene loci have so far been implicated in amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disorder characterized by progressive neurodegeneration of motor neurons (MN) and death. Most of this distinct set of ALS-related proteins undergoes toxic deposition specifically in MN for reasons which remain unclear. Here we overview a recent body of evidence indicative that mutations in ALS-related proteins can disrupt fundamental Ca2+ signalling pathways in MN, and that Ca2+ itself impacts both directly or indirectly in many ALS critical proteins and cellular processes that result in MN neurodegeneration. We argue that the inherent vulnerability of MN to dysregulation of intracellular Ca2+ is deeply associated with discriminating pathogenicity and aberrant crosstalk of most of the critical proteins involved in ALS. Overall, Ca2+ deregulation in MN is at the cornerstone of different ALS processes and is likely one of the factors contributing to the selective susceptibility of these cells to this particular neurodegenerative disease.

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“…A proteomic screen revealed that MATR3 binds to calmodulin and it was suggested that it is cleaved by both caspase-3 and caspase-8 [10]. MATR3 levels decrease after treatment with soy extract of homocysteine-stressed endothelial cells [11], and are reduced in the brain of Down syndrome fetuses [12].…”

Section: Introductionmentioning

confidence: 99%

Matrin 3 Binds and Stabilizes mRNA

et al. 2011

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Matrin 3 (MATR3) is a highly conserved, inner nuclear matrix protein with two zinc finger domains and two RNA recognition motifs (RRM), whose function is largely unknown. Recently we found MATR3 to be phosphorylated by the protein kinase ATM, which activates the cellular response to double strand breaks in the DNA. Here, we show that MATR3 interacts in an RNA-dependent manner with several proteins with established roles in RNA processing, and maintains its interaction with RNA via its RRM2 domain. Deep sequencing of the bound RNA (RIP-seq) identified several small noncoding RNA species. Using microarray analysis to explore MATR3′s role in transcription, we identified 77 transcripts whose amounts depended on the presence of MATR3. We validated this finding with nine transcripts which were also bound to the MATR3 complex. Finally, we demonstrated the importance of MATR3 for maintaining the stability of several of these mRNA species and conclude that it has a role in mRNA stabilization. The data suggest that the cellular level of MATR3, known to be highly regulated, modulates the stability of a group of gene transcripts.

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Matrin 3 is a Ca2+/calmodulin-binding protein cleaved by caspases

Cited by 30 publications

References 19 publications

In vitro selection of proteins with desired characteristics using mRNA-display

In vitro selection of proteins with desired characteristics using mRNA-display

Calcium dysregulation links ALS defective proteins and motor neuron selective vulnerability

Matrin 3 Binds and Stabilizes mRNA

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