The EMILIN/Multimerin family.

Frontiers in Immunology
Alfonso ColombattiGennaro Esposito

Abstract

Elastin microfibrillar interface proteins (EMILINs) and Multimerins (EMILIN1, EMILIN2, Multimerin1, and Multimerin2) constitute a four member family that in addition to the shared C-terminus gC1q domain typical of the gC1q/TNF superfamily members contain a N-terminus unique cysteine-rich EMI domain. These glycoproteins are homotrimeric and assemble into high molecular weight multimers. They are predominantly expressed in the extracellular matrix and contribute to several cellular functions in part associated with the gC1q domain and in part not yet assigned nor linked to other specific regions of the sequence. Among the latter is the control of arterial blood pressure, the inhibition of Bacillus anthracis cell cytotoxicity, the promotion of cell death, the proangiogenic function, and a role in platelet hemostasis. The focus of this review is to highlight the multiplicity of functions and domains of the EMILIN/Multimerin family with a particular emphasis on the regulatory role played by the ligand-receptor interactions of the gC1q domain. EMILIN1 is the most extensively studied member both from the structural and functional point of view. The structure of the gC1q of EMILIN1 solved by NMR highlights unique characteristics compar...Continue Reading

Citations

Dec 3, 2014·Matrix Biology : Journal of the International Society for Matrix Biology·Simonetta BotRoberto Doliana
Mar 8, 2016·The Journal of Investigative Dermatology·Alvise SchiavinatoGerhard Sengle
Mar 10, 2015·Frontiers in Microbiology·Veljko VeljkovicAlfonso Colombatti
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Nov 4, 2016·International Journal of Molecular Sciences·Maurizio MongiatAlice Paulitti
Mar 8, 2019·International Journal of Cosmetic Science·R FitoussiK Vié
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Jul 19, 2017·Scientific Reports·Alvise SchiavinatoGerhard Sengle
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Jul 10, 2021·Proteomics. Clinical Applications·Richard D SembaAlka Mahale
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Datasets Mentioned

BETA
GM6001

Methods Mentioned

BETA
infrared spectroscopy
NMR
X-ray
two-hybrid

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