MARCKS Is Necessary for Netrin-DCC Signaling and Corpus Callosum Formation

Brudvig, Jon; Cain, Jacob T.; Schmidt-Grimminger, G. G.; Stumpo, Deborah J.; Roux, Kyle J.; Blackshear, Perry J.; Weimer, Jill M.

doi:10.1007/s12035-018-0990-3

Cited by 18 publications

(17 citation statements)

References 53 publications

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“…The autophosphorylation and activation of FAK also requires binding to phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2 , PIP2] at the membrane ( Zhou et al, 2015 ). Intriguingly, FAK and SFK are maintained in a ready pool when not phosphorylated by the membrane-associated scaffolding protein myristoylated alanine-rich C kinase substrate (MARCKS) ( Brudvig et al, 2018 ), which interacts with PIP2 and β-actin and promotes lamellipodium formation ( Yamaguchi et al, 2009 ). This provides another link between the actin cytoskeleton and the membrane to transduce internal mechanical forces to the cell surface for remodeling, through the interaction between FAK and actin.…”

Section: Netrin-1 Receptors and Their Mechanismsmentioning

confidence: 99%

Revisiting Netrin-1: One Who Guides (Axons)

Boyer¹,

Gupton²

2018

Front. Cell. Neurosci.

143

130

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Proper patterning of the nervous system requires that developing axons find appropriate postsynaptic partners; this entails microns to meters of extension through an extracellular milieu exhibiting a wide range of mechanical and chemical properties. Thus, the elaborate networks of fiber tracts and non-fasciculated axons evident in mature organisms are formed via complex pathfinding. The macroscopic structures of axon projections are highly stereotyped across members of the same species, indicating precise mechanisms guide their formation. The developing axon exhibits directionally biased growth toward or away from external guidance cues. One of the most studied guidance cues is netrin-1, however, its presentation in vivo remains debated. Guidance cues can be secreted to form soluble or chemotactic gradients or presented bound to cells or the extracellular matrix to form haptotactic gradients. The growth cone, a highly specialized dynamic structure at the end of the extending axon, detects these guidance cues via transmembrane receptors, such as the netrin-1 receptors deleted in colorectal cancer (DCC) and UNC5. These receptors orchestrate remodeling of the cytoskeleton and cell membrane through both chemical and mechanotransductive pathways, which result in traction forces generated by the cytoskeleton against the extracellular environment and translocation of the growth cone. Through intracellular signaling responses, netrin-1 can trigger either attraction or repulsion of the axon. Here we review the mechanisms by which the classical guidance cue netrin-1 regulates intracellular effectors to respond to the extracellular environment in the context of axon guidance during development of the central nervous system and discuss recent findings that demonstrate the critical importance of mechanical forces in this process.

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Section: Netrin-1 Receptors and Their Mechanismsmentioning

confidence: 99%

Revisiting Netrin-1: One Who Guides (Axons)

Boyer¹,

Gupton²

2018

Front. Cell. Neurosci.

143

130

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“…Since its development and initial application in 2012 (7), BioID has been cited and/or applied in over 200 PubMed-published articles and has been utilized in several unicellular organisms (see (12–15) for examples), mammalian cells (5), plants (16,17), and mice (18–20), including compartmental proteomics of a parasitic organism infecting mice (21). Novel or improved applications using BioID ligase have spurred numerous follow-up articles including a smaller version of BioID with improved sensitivity and localization (22), its use for identifying protein-RNA interactions (23), split-BioID studies (24,25), and faster versions of BioID (26).…”

Section: Introductionmentioning

confidence: 99%

BioID as a Tool for Protein-Proximity Labeling in Living Cells

Sears

May

Roux

2019

Methods in Molecular Biology

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BioID has become an increasingly utilized tool for identifying candidate protein-protein interactions (PPIs) in living cells. This method utilizes a promiscuous biotin ligase, called BioID, fused to a protein-of-interest that when expressed in cells can be induced to biotinylate interacting and proximate proteins over a period of hours, thus generating a history of protein associations. These biotinylated proteins are subsequently purified and identified via mass spectrometry. Compared to other conventional methods typically used to screen strong PPIs, BioID allows for the detection of weak and transient interactions within a relevant biological setting over a defined period of time. Here we briefly review the scientific progress enabled by the BioID technology, detail an updated protocol for applying the method to proteins in living cells, and offer insights for troubleshooting commonly encountered setbacks.

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“…during tumor cell invasion, has been debated for years. As proximity-dependent approaches can also be applied in vivo [73][74][75] , our study opens the door to the development of proximity-dependent labeling approaches in in vivo models of invasion more relevant to metastatic progression.…”

Section: Discussionmentioning

confidence: 98%

A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells

Thuault

Mamelonet

Salameh

et al. 2020

Sci Rep

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Supplementary Table S1: List of proteins biotinylated by Tks5-BirA* fusion protein. Protein list results from the comparison of proteins biotinylated by Tks5-BirA* fusion protein with proteins biotinylated by BirA* control protein, after their isolation by affinity capture and identification by mass spectrometry. Proteins listed here correspond to proteins above the full line indicative of protein hits obtained at a pFDR of 1% on Fig.3A volcano plot. For each protein their link to invadosome, their implication in actin cytoskeleton organization and their link to cancer invasion and metastasis have been analyzed, by comparison to the list of proteins obtained for "invadosome" query by GLAD4U literature mining and manual literature searching. The presence of Proline-rich regions and SH3 domains determined by InterPro site is also referenced. Data result from two different experiments processed three times. Supplementary Table S2: List of proteins biotinylated by PX-Tks5-BirA* fusion protein. Protein list results from the comparison of proteins biotinylated by PX-Tks5-BirA* fusion protein with proteins biotinylated by BirA* control protein, after their isolation by affinity capture and identification by mass spectrometry. Proteins listed here correspond to proteins hits obtained at a pFDR of 1%. Data result from two different experiments processed three times.

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MARCKS Is Necessary for Netrin-DCC Signaling and Corpus Callosum Formation

Cited by 18 publications

References 53 publications

Revisiting Netrin-1: One Who Guides (Axons)

Revisiting Netrin-1: One Who Guides (Axons)

BioID as a Tool for Protein-Proximity Labeling in Living Cells

A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells

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