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Structural basis of semaphorin–plexin signalling [PDF]
Nature, 2010 Cell-cell signalling of semaphorin ligands through interaction with plexin receptors is important for the homeostasis and morphogenesis of many tissues and is widely studied for its role in neural connectivity, cancer, cell migration and immune responses. SEMA4D and Sema6A exemplify two diverse vertebrate, membrane-spanning semaphorin classes (4 and 6)
Bert J C Janssen +2 more
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Identification and characterization of a novel mouse plexin, plexin-A4
Mechanisms of Development, 2003 Plexins belonging to the plexin-A subfamily form complexes with neuropilins and propagate signals of class 3 semaphorins into neurons, even though they do not directly bind the semaphorins. In this study, we identified a new member of the plexin-A subfamily in the mice, plexin-A4, and showed that it was expressed in the developing nervous system with a
Fumikazu Suto +2 more
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Structural mechanisms of plexin signaling [PDF]
Progress in Biophysics and Molecular Biology, 2015 Signaling through plexin, the major cell surface receptor for semaphorin, plays critical roles in regulating processes such as neuronal axon guidance, angiogenesis and immune response. Plexin is normally kept inactive in the absence of semaphorin. Upon binding of semaphorin to the extracellular region, plexin is activated and transduces signal to the ...
Xuewu Zhang
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Divergent roles of Plexin D1 in cancer
Biochimica Et Biophysica Acta: Reviews on Cancer, 2019 Plexin D1 belongs to a family of transmembrane proteins called plexins. It was characterized as a receptor for semaphorins and is known to be essential for axonal guidance and vascular patterning. Mutations in Plexin D1 have been implicated in pathologic conditions such as truncus arteriosus and Möbius syndrome.
Debabrata Mukhopadhyay
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Plexin-A1 and plexin-B1 specifically interact at their cytoplasmic domains
Biochemical and Biophysical Research Communications, 2003Semaphorin 3A (Sema3A) is a member of semaphorins and functions as an axonal repulsive guidance molecule. Neuropilin-1 and plexin-As form receptor complexes for Sema3A and plexin-As are thought to initiate the intracellular signaling cascade. However, the molecule by which plexin-As transduce their signal is not well understood.
Hiroshi, Usui +3 more
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Semaphorins and plexins as therapeutic targets
Nature Reviews Drug Discovery, 2014Semaphorins are membrane-bound or diffusible factors that regulate key cellular functions and are involved in cell-cell communication. Most of the effects of semaphorins are mediated by plexins. Work over the past decade has revealed crucial functions of the semaphorin-plexin system in mammalian physiology. It has also become clear that semaphorins and
Thomas, Worzfeld, Stefan, Offermanns
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Plexins are partners for neuropilins
Science Signaling, 1999Membrane-bound and secreted semaphorins regulate a number of cell adhesion processes including axon guidance in the nervous system. However, little is known about the receptors to which they bind. Although neuropilins bind to secreted class 3 semaphorins (Sema3), it is thought that a coreceptor might be required to transduce Sema3 signals
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Plexins: axon guidance and signal transduction
Cellular and Molecular Life Sciences, 2005Axon guidance represents a key stage in the formation of neuronal network. Axons are guided by a variety of guidance factors, such as semaphorins, ephrins and netrin. Plexins function as receptors for the repulsive axonal guidance molecules semaphorins.
M, Negishi, I, Oinuma, H, Katoh
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The expression of plexins during mouse embryogenesis
Gene Expression Patterns, 2005Plexins are large transmembrane proteins that are receptors for semaphorins, either alone or in a complex with neuropilin-1 or -2. Nine different mouse plexins have been found: Plexin-A1-4, -B1-3, -C1 and -D1. The expression and function of plexins in non-neuronal tissues has been poorly characterized, although Plexin-A1 has been shown to have a role ...
Nina M, Perälä +2 more
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Identification of Plexin Family Molecules in Mice
Biochemical and Biophysical Research Communications, 1996By screening of E17.5 mouse brain cDNA libraries, we isolated two cDNAs encoding new plexin-like proteins. Sequencing revealed that these two proteins were type 1 membrane proteins which showed over 60% identity at the amino acid level to mouse plexin 1.
T, Kameyama +6 more
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