Dual Functions of Dab1 during Brain Development

Li, Feng; Cooper, Jonathan A.

doi:10.1128/mcb.00663-08

Cited by 55 publications

(75 citation statements)

References 40 publications

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“…Tyrosine-phosphorylated Dab1 acts as a hub to recruit different Src homology 2 (SH2) domain-containing proteins, including the p85 regulatory subunit of phosphatidylinositide-3-kinase (PI3K), cellular adaptors CrkL, Crk, Nckβ and SOCS (suppressor of cytokine signaling) [30,[33][34][35][36][37]. Different tyrosine residues appear to interact with distinct SH2 domains: Y 220 and Y 232 are required for the recruitment of SH2 domains from Crk, CrkL and Nckβ adaptor proteins [30,[35][36][37], whereas Y 185 and Y 198 are necessary for the recruitment of PI3K and SOCS SH2 domains [33][34].…”

Section: Dab1 Is a Crucial Cellular Adaptor In Reelin Signalingmentioning

confidence: 99%

“…Different tyrosine residues appear to interact with distinct SH2 domains: Y 220 and Y 232 are required for the recruitment of SH2 domains from Crk, CrkL and Nckβ adaptor proteins [30,[35][36][37], whereas Y 185 and Y 198 are necessary for the recruitment of PI3K and SOCS SH2 domains [33][34]. Tyrosine-phosphorylated Dab1 also interacts with the microtubule associated protein, Lis1, albeit in a SH2 domain-independent manner [38].…”

Section: Dab1 Is a Crucial Cellular Adaptor In Reelin Signalingmentioning

confidence: 99%

“…Dab1-Crk-C3G-Rap1-cadherin pathway Reelin promotes Dab1 (at Y220 and Y232 tyrosine phosphorylation sites)-Crk interaction, induces tyrosine phosphorylation of C3G (a guanine nucleotide exchange factor for Rap1) and activates the small GTPase Rap1 [30,34,[36][37]. Ablation of CrkII −/− CrkL −/− in mouse cortex generates a reeler-like phenotype without affecting Reelin-induced Dab1 tyrosine phosphorylation [39].…”

Section: Dab1 Tyrosine Phosphorylation Activates Downstream Signalingmentioning

confidence: 99%

“…A direct consequence of expressing such Dab1 isoforms would be altered phosphotyrosine-associated interactions resulting from modified tyrosine phosphorylation status. Previous studies have suggested that the YQXI and YQXP motifs in Dab1 have distinct functions in Reelin signaling [33][34]. YQXI motifs are important for both turning on and turning off downstream pathways by activating PI3K-Akt and triggering Cul5-mediated proteasome degradation of Dab1 [33][34].…”

Section: Alternative Splicing Regulates Dab1 Function Alternative Splmentioning

confidence: 99%

“…YQXI motifs are important for both turning on and turning off downstream pathways by activating PI3K-Akt and triggering Cul5-mediated proteasome degradation of Dab1 [33][34]. YQVP motifs appear to be critical in recruiting Crk and Nck adaptors to form a signaling scaffold complex [30,[34][35][36][37].…”

Section: Alternative Splicing Regulates Dab1 Function Alternative Splmentioning

confidence: 99%

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Reelin-Disabled-1 signaling in neuronal migration: splicing takes the stage

Gao

Godbout

2012

Cell. Mol. Life Sci.

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Reelin-Disabled-1 (Dab1) signaling has a well-established role in regulating neuronal migration during brain development. Binding of Reelin to its receptors induces Dab1 tyrosine phosphorylation. Tyrosine-phosphorylated Dab1 recruits a wide range of SH2 domain-containing proteins and activates multiple signaling cascades, resulting in cytoskeleton remodeling and precise neuronal positioning. In this review, we summarize recent progress in the Reelin-Dab1 signaling field. We focus on Dab1 alternative splicing as a mechanism for modulating the Reelin signal in developing brain. We suggest that correct positioning of neurons in the developing brain is at least partly controlled by alternatively-spliced Dab1 isoforms that differ in the number and type of tyrosine phosphorylation motifs that they contain. We propose a model whereby different subsets of SH2 domain-containing proteins are activated by different Dab1 isoforms, resulting in coordinated migration of neurons.

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Section: Dab1 Is a Crucial Cellular Adaptor In Reelin Signalingmentioning

confidence: 99%

Section: Dab1 Is a Crucial Cellular Adaptor In Reelin Signalingmentioning

confidence: 99%

Section: Dab1 Tyrosine Phosphorylation Activates Downstream Signalingmentioning

confidence: 99%

Section: Alternative Splicing Regulates Dab1 Function Alternative Splmentioning

confidence: 99%

Section: Alternative Splicing Regulates Dab1 Function Alternative Splmentioning

confidence: 99%

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Reelin-Disabled-1 signaling in neuronal migration: splicing takes the stage

Gao

Godbout

2012

Cell. Mol. Life Sci.

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CRK and NCK adaptors may functionally overlap in zebrafish neurodevelopment, as indicated by common binding partners and overlapping expression patterns

Stergas,

Dillon‐Martin,

Dumas

et al. 2023

FEBS Letters

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CRK adaptor proteins are important for signal transduction mechanisms driving cell proliferation and positioning during vertebrate central nervous system development. Zebrafish lacking both CRK family members exhibit small, disorganized retinas with 50% penetrance. The goal of this study was to determine whether another adaptor protein might functionally compensate for the loss of CRK adaptors. Expression patterns in developing zebrafish, and bioinformatic analyses of the motifs recognized by their SH2 and SH3 domains, suggest NCK adaptors are well‐positioned to compensate for loss of CRK adaptors. In support of this hypothesis, proteomic analyses found CRK and NCK adaptors share overlapping interacting partners including known regulators of cell adhesion and migration, suggesting their functional intersection in neurodevelopment.

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Development and distribution of neuronal cilia in mouse neocortex

Arellano

Guadiana

Breunig

et al. 2012

J of Comparative Neurology

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Neuronal primary cilia are not generally recognized, but they are considered to extend from most, if not all, neurons in the neocortex. However, when and how cilia develop in neurons are not known. This study used immunohistochemistry for adenylyl cyclase III (ACIII), a marker of primary cilia, and electron microscopic analysis to describe the development and maturation of cilia in mouse neocortical neurons. Our results indicate that ciliogenesis is initiated in late fetal stages after neuroblast migration, when the mother centriole docks with the plasma membrane, becomes a basal body, and grows a cilia bud that we call a procilium. This procilium consists of a membranous protrusion extending from the basal body but lacking axonemal structure and remains undifferentiated until development of the axoneme and cilia elongation starts at about postnatal day 4. Neuronal cilia elongation and final cilia length depend on layer position, and the process extends for a long time, lasting 8–12 weeks. We show that, in addition to pyramidal neurons, inhibitory interneurons also grow cilia of comparable length, suggesting that cilia are indeed present in all neocortical neuron subtypes. Furthermore, the study of mice with defective ciliogenesis suggested that failed elongation of cilia is not essential for proper neuronal migration and laminar organization or establishment of neuronal polarity. Thus, the function of this organelle in neocortical neurons remains elusive.

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Dual Functions of Dab1 during Brain Development

Cited by 55 publications

References 40 publications

Reelin-Disabled-1 signaling in neuronal migration: splicing takes the stage

Reelin-Disabled-1 signaling in neuronal migration: splicing takes the stage

CRK and NCK adaptors may functionally overlap in zebrafish neurodevelopment, as indicated by common binding partners and overlapping expression patterns

Development and distribution of neuronal cilia in mouse neocortex

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