CELSR1 Membrane Protein Introduction

Introduction of CELSR1

CELSR1, also known as flamingo homolog 2 (hFmi2) or cadherin family member 9 (CDHF9), is a membrane protein belongs to the flamingo subfamily, part of the cadherin superfamily. The flamingo subfamily which is a subpopulation that does not interact with catenins comprise several nonclassic-type cadherins. The flamingo cadherins are located at the plasma membrane and consist of nine cadherin domains, two laminin G-like domains in their ectodomain, and seven epidermal growth factor-like repeats. The unique characteristic of this subfamily is that they have seven transmembrane domains.

Function of CELSR1 Membrane Protein

CELSR1 was found to be endogenously expressed in human aortic endothelial cells (HAEC) and human umbilical vein endothelial cells (HUVEC). And it is a pivotal component of the noncanonical Wnt/planar cell polarity (PCP) pathway which critically modulates endothelial cell proliferation and angiogenesis. Thus, CELSR1 is supposed to play a crucial role in regulating multiple phenotypes of endothelial cells, including migration, proliferation, and formation of capillary-like structures. Furthermore, Wnt /PCP signaling pathway is proved to be implicated in human carcinogenesis. Antibody, RNAi, or small molecule compounds that regulate the function of Wnt /PCP signaling molecules, including CELSR1, are potential candidates for novel cancer therapeutics. CELSR1 may also play an essential role in cell-cell signaling during nervous system formation. Specifically, CELSR1 is supposed to be involved in contact-mediated communication, with cadherin domains functioning as homophilic binding regions and the EGF-like domains contributing to cell adhesion and receptor-ligand interactions.

Fig.1 Domain architecture of CELSR1. (Wang, 2014)

Application of CELSR1 Membrane Protein in Literature

1. Duncan J.S., et al. Celsr1 coordinates the planar polarity of vestibular hair cells during inner ear development. Dev Biol. 2017, 423(2): 126-137. PubMed ID: 28159525

This article reports that Celsr1 is asymmetrically distributed at cell boundaries between hair cells and neighboring supporting cells in the developing vestibular and auditory sensory epithelia.

2. Glasco D.M., et al. The atypical cadherin Celsr1 functions non-cell autonomously to block rostral migration of facial branchiomotor neurons in mice. Dev Biol. 2016, 417(1): 40-9. PubMed ID: 27395006

This article suggests strongly that Celsr1 ensures that FBM neurons migrate caudally by suppressing molecular cues in the rostral hindbrain that can attract FBM neurons.

3. Zhan Y.H., et al. CELSR1 Is a Positive Regulator of Endothelial Cell Migration and Angiogenesis. Biochemistry (Mosc). 2016, 81(6): 591-9. PubMed ID: 27301287

Authors in this group evaluate the biological significance of CELSR1 in endothelial cell migration and angiogenesis and show that CELSR1 plays an important role in regulating multiple phenotypes of endothelial cells, including proliferation, migration, and formation of capillary-like structures.

4. Shi D., et al. Celsr1 is required for the generation of polarity at multiple levels of the mouse oviduct. Development. 2014, 141(23): 4558-68. PubMed ID: 2540639

This article focuses on the pharmacological activation of adenosine signaling in β-cell proliferation in zebrafish. It shows that A2a receptor plays an important role in adenosine signaling and compensatory β-cell proliferation. Meanwhile, this feature can be used in future therapeutic development for diabetes.

5. Tatin F., et al. Planar cell polarity protein Celsr1 regulates endothelial adherens junctions and directed cell rearrangements during valve morphogenesis. Dev Cell. 2013, 26(1): 31-44. PubMed ID: 23792146

This article shows a critical role for the core planar cell polarity (PCP) proteins Celsr1 and Vangl2 in the complex morphogenetic process of intraluminal valve formation in lymphatic vessels. PCP signaling controls tissue morphogenesis by coordinating collective cell behaviors.

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Reference

1. Wang X J., et al. (2014). Understanding cadherin EGF LAG seven-pass G-type receptors. Journal of neurochemistry. 131(6), 699-711.

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