Dab1 and reelin participate in a common signal pathway that controls intestinal crypt/villus unit dynamics

Vázquez‐Carretero, María D.; García‐Miranda, Pablo; Calonge, M. L.; Peral, María J.; Ilundáin, A.

doi:10.1111/boc.201300078

Cited by 10 publications

(18 citation statements)

References 38 publications

(54 reference statements)

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“…The extracellular matrix protein Reelin has been found to promote the proliferation of intestinal and submandibular gland epithelial cells and granulose cells via ApoERs (VLDLR)/Dab1/PI3K/Akt and MAPK pathways303132. Whether similar function and similar signaling pathways can be found in Reelin-expressing tumors are not clear.…”

Section: Discussionmentioning

confidence: 99%

Extracellular matrix protein Reelin promotes myeloma progression by facilitating tumor cell proliferation and glycolysis

Qin

Lin

Cao

et al. 2017

Sci Rep

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Reelin is an extracellular matrix protein that is crucial for neuron migration, adhesion, and positioning. We examined the expression of Reelin in a large cohort of multiple myeloma patients recorded in Gene Expression Omnibus (GEO) database and used over-expression and siRNA knockdown of Reelin to investigate the role of Reelin in myeloma cell growth. We find that Reelin expression is negatively associated with myeloma prognosis. Reelin promotes myeloma cell proliferation in vitro as well as in vivo. The Warburg effect, evidenced by increased glucose uptake and lactate production, is also enhanced in Reelin-expressing cells. The activation of FAK/Syk/Akt/mTOR and STAT3 pathways contributes to Reelin-induced cancer cell growth and metabolic reprogramming. Our findings further reveal that activated Akt and STAT3 pathways induce the upregulation of HIF1α and its downstream targets (LDHA and PDK1), leading to increased glycolysis in myeloma cells. Together, our results demonstrate the critical contributions of Reelin to myeloma growth and metabolism. It presents an opportunity for myeloma therapeutic intervention by inhibiting Reelin and its signaling pathways.

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Section: Discussionmentioning

confidence: 99%

Extracellular matrix protein Reelin promotes myeloma progression by facilitating tumor cell proliferation and glycolysis

Qin

Lin

Cao

et al. 2017

Sci Rep

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“…Furthermore, Dab1 has been implicated in the regulation of cholesterol efflux in RAW 264.7 mouse macrophage cell line [24]. Vázquez-Carretero et al have reported that Dab1 participates in regulation of intestinal crypt/villus unit dynamics [25]. In addition, Dab1 is involved in regulation of mammary gland development, cartilage and tendon differentiation, odontogenesis, and granulosa cell proliferation in chicken follicle [26–30].…”

Section: Discussionmentioning

confidence: 99%

Dab1 Contributes to Angiotensin II-Induced Apoptosis via p38 Signaling Pathway in Podocytes

Gao

Chen

Zhu

et al. 2017

BioMed Research International

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Numerous studies have found that angiotensin II (Ang II) participates in podocyte apoptosis and exacerbates progression of end-stage kidney disease (ESKD). However, its underlying mechanism remains largely unexplored. As a homolog of Drosophila disabled (Dab) protein, Dab1 plays a vital role in cytoskeleton, neuronal migration, and proliferation. In the present study, our data revealed that Ang II-infused rats developed hypertension, proteinuria, and podocyte injury accompanied by Dab1 phosphorylation and increased reelin expression in kidney. Moreover, Ang II induced podocyte apoptosis in vitro. Dab1 phosphorylation and reelin expression in podocytes were increased after exposure to Ang II. Conversely, Dab1 small interfering RNA (siRNA) exerted protective effects on Ang II-induced podocyte apoptosis, resulting in decreased p38 phosphorylation and reelin expression. These results indicated that Dab1 mediated Ang II-induced podocyte apoptosis via p38 signaling pathway.

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“…Opto-Dab1 may also be useful to study Reelin-Dab1 signaling in synaptic plasticity140, in the development of non-neuronal tissues, such as mammary gland, small intestine and limbs, and in diseases including cancer414243. These applications will require the development of techniques to express opto-Dab1 effectively in the target cell types and to direct light to the respective tissues.…”

Section: Discussionmentioning

confidence: 99%

Optogenetic control of the Dab1 signaling pathway

Wang

Cooper

2017

Sci Rep

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The Reelin-Dab1 signaling pathway regulates development of the mammalian brain, including neuron migrations in various brain regions, as well as learning and memory in adults. Extracellular Reelin binds to cell surface receptors and activates phosphorylation of the intracellular Dab1 protein. Dab1 is required for most effects of Reelin, but Dab1-independent pathways may contribute. Here we developed a single-component, photoactivatable Dab1 (opto-Dab1) by using the blue light-sensitive dimerization/oligomerization property of A. thaliana Cryptochrome 2 (Cry2). Opto-Dab1 can activate downstream signals rapidly, locally, and reversibly upon blue light illumination. The high spatiotemporal resolution of the opto-Dab1 probe also allows us to control membrane protrusion, retraction and ruffling by local illumination in both COS7 cells and in primary neurons. This shows that Dab1 activation is sufficient to orient cell movement in the absence of other signals. Opto-Dab1 may be useful to study the biological functions of the Reelin-Dab1 signaling pathway both in vitro and in vivo.

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Dab1 and reelin participate in a common signal pathway that controls intestinal crypt/villus unit dynamics

Abstract: All together, the current findings link reelin with Dab1 and suggest that Dab1 functions downstream of reelin action on the homeostasis of the crypt-villus unit.

Cited by 10 publications

References 38 publications

Extracellular matrix protein Reelin promotes myeloma progression by facilitating tumor cell proliferation and glycolysis

Extracellular matrix protein Reelin promotes myeloma progression by facilitating tumor cell proliferation and glycolysis

Dab1 Contributes to Angiotensin II-Induced Apoptosis via p38 Signaling Pathway in Podocytes

Optogenetic control of the Dab1 signaling pathway

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