Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors

Summary: Projections from sensory neurons of olfactory systems coalesce into glomeruli in the brain. The Kirrel receptors are believed to homodimerize via their ectodomains and help separate sensory neuron axons into Kirrel2- or Kirrel3-expressing glomeruli. Here, we present the crystal structures o...

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Autores principales:	Jing Wang, Neelima Vaddadi, Joseph S. Pak, Yeonwoo Park, Sabrina Quilez, Christina A. Roman, Emilie Dumontier, Joseph W. Thornton, Jean-François Cloutier, Engin Özkan
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	accessory olfactory system axonal coalescence cell adhesion molecule glomeruli Kirrel2 Kirrel3 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/ea566befb1714a608858eb1ec6016712
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spelling	oai:doaj.org-article:ea566befb1714a608858eb1ec60167122021-11-04T04:29:30ZMolecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors2211-124710.1016/j.celrep.2021.109940https://doaj.org/article/ea566befb1714a608858eb1ec60167122021-11-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2211124721014133https://doaj.org/toc/2211-1247Summary: Projections from sensory neurons of olfactory systems coalesce into glomeruli in the brain. The Kirrel receptors are believed to homodimerize via their ectodomains and help separate sensory neuron axons into Kirrel2- or Kirrel3-expressing glomeruli. Here, we present the crystal structures of homodimeric Kirrel receptors and show that the closely related Kirrel2 and Kirrel3 have evolved specific sets of polar and hydrophobic interactions, respectively, disallowing heterodimerization while preserving homodimerization, likely resulting in proper segregation and coalescence of Kirrel-expressing axons into glomeruli. We show that the dimerization interface at the N-terminal immunoglobulin (IG) domains is necessary and sufficient to create homodimers and fail to find evidence for a secondary interaction site in Kirrel ectodomains. Furthermore, we show that abolishing dimerization of Kirrel3 in vivo leads to improper formation of glomeruli in the mouse accessory olfactory bulb as observed in Kirrel3−/− animals. Our results provide evidence for Kirrel3 homodimerization controlling axonal coalescence.Jing WangNeelima VaddadiJoseph S. PakYeonwoo ParkSabrina QuilezChristina A. RomanEmilie DumontierJoseph W. ThorntonJean-François CloutierEngin ÖzkanElsevierarticleaccessory olfactory systemaxonal coalescencecell adhesion moleculeglomeruliKirrel2Kirrel3Biology (General)QH301-705.5ENCell Reports, Vol 37, Iss 5, Pp 109940- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	accessory olfactory system axonal coalescence cell adhesion molecule glomeruli Kirrel2 Kirrel3 Biology (General) QH301-705.5
spellingShingle	accessory olfactory system axonal coalescence cell adhesion molecule glomeruli Kirrel2 Kirrel3 Biology (General) QH301-705.5 Jing Wang Neelima Vaddadi Joseph S. Pak Yeonwoo Park Sabrina Quilez Christina A. Roman Emilie Dumontier Joseph W. Thornton Jean-François Cloutier Engin Özkan Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors
description	Summary: Projections from sensory neurons of olfactory systems coalesce into glomeruli in the brain. The Kirrel receptors are believed to homodimerize via their ectodomains and help separate sensory neuron axons into Kirrel2- or Kirrel3-expressing glomeruli. Here, we present the crystal structures of homodimeric Kirrel receptors and show that the closely related Kirrel2 and Kirrel3 have evolved specific sets of polar and hydrophobic interactions, respectively, disallowing heterodimerization while preserving homodimerization, likely resulting in proper segregation and coalescence of Kirrel-expressing axons into glomeruli. We show that the dimerization interface at the N-terminal immunoglobulin (IG) domains is necessary and sufficient to create homodimers and fail to find evidence for a secondary interaction site in Kirrel ectodomains. Furthermore, we show that abolishing dimerization of Kirrel3 in vivo leads to improper formation of glomeruli in the mouse accessory olfactory bulb as observed in Kirrel3−/− animals. Our results provide evidence for Kirrel3 homodimerization controlling axonal coalescence.
format	article
author	Jing Wang Neelima Vaddadi Joseph S. Pak Yeonwoo Park Sabrina Quilez Christina A. Roman Emilie Dumontier Joseph W. Thornton Jean-François Cloutier Engin Özkan
author_facet	Jing Wang Neelima Vaddadi Joseph S. Pak Yeonwoo Park Sabrina Quilez Christina A. Roman Emilie Dumontier Joseph W. Thornton Jean-François Cloutier Engin Özkan
author_sort	Jing Wang
title	Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors
title_short	Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors
title_full	Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors
title_fullStr	Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors
title_full_unstemmed	Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors
title_sort	molecular and structural basis of olfactory sensory neuron axon coalescence by kirrel receptors
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/ea566befb1714a608858eb1ec6016712
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_version_	1718445305966362624

Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors

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