Novel role for the Lu/BCAM–spectrin interaction in actin cytoskeleton reorganization

Collec, Emmanuel; Lecomte, Marie‐Christine; Nemer, Wassim El; Colin, Yves; Kim, Caroline Le Van

doi:10.1042/bj20101717

Cited by 23 publications

(21 citation statements)

References 41 publications

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“…Furthermore, conserved TEAD-binding sites were found in the promoters of Bcam , S1pr2 and Nuak2 (Figure 5C), where the YAP and TEAD proteins reside as revealed by ChIP-Seq and ChIP-qPCR analysis (Figure 5E). BCAM and S1PR2 can activate RhoA (Collec et al, 2011; Randriamboavonjy et al, 2009) to promote pMLC production. The NUAK2 kinase can also enhance pMLC generation by inhibiting MLC phosphatase independently of RhoA (Zagórska et al, 2010).…”

Section: Resultsmentioning

confidence: 99%

YAP is essential for mechanical force production and epithelial cell proliferation during lung branching morphogenesis

Lin

Yao

Zhang

et al. 2017

eLife

112

114

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Branching morphogenesis is a fundamental program for tissue patterning. We show that active YAP, a key mediator of Hippo signaling, is distributed throughout the murine lung epithelium and loss of epithelial YAP severely disrupts branching. Failure to branch is restricted to regions where YAP activity is removed. This suggests that YAP controls local epithelial cell properties. In support of this model, mechanical force production is compromised and cell proliferation is reduced in Yap mutant lungs. We propose that defective force generation and insufficient epithelial cell number underlie the branching defects. Through genomic analysis, we also uncovered a feedback control of pMLC levels, which is critical for mechanical force production, likely through the direct induction of multiple regulators by YAP. Our work provides a molecular pathway that could control epithelial cell properties required for proper morphogenetic movement and pattern formation.DOI: http://dx.doi.org/10.7554/eLife.21130.001

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Section: Resultsmentioning

confidence: 99%

YAP is essential for mechanical force production and epithelial cell proliferation during lung branching morphogenesis

Lin

Yao

Zhang

et al. 2017

eLife

112

114

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“…The Arg 573 Lys 574 motif in the shared cytoplasmic tail of Lu and B-CAM attaches to the spectrin cytoskeleton and regulates cell adhesive activity (32,33). A recent study showed that a Lu/B-CAM-␣II spectrin interaction impacts actin organization in epithelial cells (34). This motif in Lu/B-CAM may be involved in intracellular signaling that mediates cell migration on LM-511.…”

Section: Discussionmentioning

confidence: 99%

The Lutheran/Basal Cell Adhesion Molecule Promotes Tumor Cell Migration by Modulating Integrin-mediated Cell Attachment to Laminin-511 Protein

Kikkawa

Ogawa

Sudo

et al. 2013

Journal of Biological Chemistry

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Background: Lu/B-CAM is a specific receptor for laminin ␣5, a subunit of laminin-511 (LM-511) that is a major component of basement membranes. Results: Expression of Lu/B-CAM promotes tumor cell migration on LM-511 rather than cell attachment. Conclusion: Tumor cell migration on LM-511 requires that Lu/B-CAM competitively weakens cell attachment through integrins. Significance: The competitive interaction of the laminin receptors may provide a balance between static and migratory cell behaviors.

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“…16,17,29,30 In sickle cell erythrocytes, release of Lu/BCAM from the spectrin network as a consequence of Lu/BCAM phosphorylation is hypothesized to increase Lu/BCAM clustering after ligand binding and therefore enhance erythrocyte adhesion to laminin-a5. 16,30 We wanted to verify whether the mobility of Lu/BCAM within the erythrocyte membrane is impacted by neuraminidase treatment.…”

Section: Loss Of Gpc Binding Does Not Increase Lu/bcam Mobility In Thmentioning

confidence: 99%

Glycophorin-C sialylation regulates Lu/BCAM adhesive capacity during erythrocyte aging

et al. 2018

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Key Points• The Lu/BCAM adhesion molecule is gradually activated during erythrocyte aging due to loss of sialic acid on glycophorin-C.• Upon activation, Lu/ BCAM engages a sialic acid-dependent interaction with the extracellular matrix protein laminin-a5.Lutheran/basal cell adhesion molecule (Lu/BCAM) is a transmembrane adhesion molecule expressed by erythrocytes and endothelial cells that can interact with the extracellular matrix protein laminin-a5. In sickle cell disease, Lu/BCAM is thought to contribute to adhesion of sickle erythrocytes to the vascular wall, especially during vaso-occlusive crises.On healthy erythrocytes however, its function is unclear. Here we report that Lu/BCAM is activated during erythrocyte aging. We show that Lu/BCAM-mediated binding to laminin-a5 is restricted by interacting, in cis, with glycophorin-C-derived sialic acid residues. Following loss of sialic acid during erythrocyte aging, Lu/BCAM is released from glycophorin-C and allowed to interact with sialic acid residues on laminin-a5.

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Novel role for the Lu/BCAM–spectrin interaction in actin cytoskeleton reorganization

Cited by 23 publications

References 41 publications

YAP is essential for mechanical force production and epithelial cell proliferation during lung branching morphogenesis

YAP is essential for mechanical force production and epithelial cell proliferation during lung branching morphogenesis

The Lutheran/Basal Cell Adhesion Molecule Promotes Tumor Cell Migration by Modulating Integrin-mediated Cell Attachment to Laminin-511 Protein

Glycophorin-C sialylation regulates Lu/BCAM adhesive capacity during erythrocyte aging

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