Rab proteins in the brain and corpus allatum of Bombyx mori

Uno, Tomohide; Furutani, Masayuki; Watanabe, Chihiro; Sakamoto, Katsuhiko; Uno, Yuichi; Kanamaru, Kengo; Yamagata, Hiroshi; Mizoguchi, Akira; Takeda, Makio

doi:10.1007/s00418-016-1422-y

Cited by 6 publications

(7 citation statements)

References 60 publications

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“…The Rab subfamily has also been related to neurodegenerative disorders such as Alzheimer’s disease and PD (Wilson et al, 2014; Saridaki et al, 2018; Yan et al, 2018). Previous studies have shown that Rab3A, Rab6, Rab8A/Rab8, Rab23, and Rab27b are highly expressed in the brain and participate in synaptic vesicle exocytosis, postsynaptic glutamate receptor dynamics, neurite growth and neural development (Takamori et al, 2006; Ng and Tang, 2008; Uno et al, 2016). Rab3 is the most abundant Rab protein in the brain.…”

Section: The Rab Subfamily In Non-neoplastic Cerebral Diseasesmentioning

confidence: 99%

The Ras Superfamily of Small GTPases in Non-neoplastic Cerebral Diseases

Qu¹,

Pan²,

et al. 2019

Front. Mol. Neurosci.

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The small GTPases from the Ras superfamily play crucial roles in basic cellular processes during practically the entire process of neurodevelopment, including neurogenesis, differentiation, gene expression, membrane and protein traffic, vesicular trafficking, and synaptic plasticity. Small GTPases are key signal transducing enzymes that link extracellular cues to the neuronal responses required for the construction of neuronal networks, as well as for synaptic function and plasticity. Different subfamilies of small GTPases have been linked to a number of non-neoplastic cerebral diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), intellectual disability, epilepsy, drug addiction, Huntington's disease (HD), amyotrophic lateral sclerosis (ALS) and a large number of idiopathic cerebral diseases. Here, we attempted to make a clearer illustration of the relationship between Ras superfamily GTPases and non-neoplastic cerebral diseases, as well as their roles in the neural system. In future studies, potential treatments for non-neoplastic cerebral diseases which are based on small GTPase related signaling pathways should be explored further. In this paper, we review all the available literature in support of this possibility.

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Section: The Rab Subfamily In Non-neoplastic Cerebral Diseasesmentioning

confidence: 99%

The Ras Superfamily of Small GTPases in Non-neoplastic Cerebral Diseases

Qu¹,

Pan²,

et al. 2019

Front. Mol. Neurosci.

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“…Bombyxin, a member of the insulin family of peptides, is synthesized in the insect brain (Iwami, Furuya, & Kataoka, 1996;Mizoguchi et al, 1987;Nagasawa et al, 1986;Nagata et al, 1992) and is an essential growth factor for wing imaginal disks in Pseudodeltote coenia and M. sexta (Nijhout & Grunert, 2002;Nijhout et al, 2007). A previous report indicated that bombyxin-ir colocalized with Rab1-ir, Rab3-ir, Rab6-ir, Rab7-ir, and Rab14-ir (Uno et al, 2016). RabX4 may be involved in the synthesis, transport, and degradation of bombyxin in the brain of B. mori, in addition to other Rabs.…”

Section: Discussionmentioning

confidence: 99%

“…To clarify the relationship between Rabs and neuropeptide secretion, we performed anatomical and immunohistochemical analysis of the B. mori brain using antibodies against Rabs. Rab1, Rab3, Rab6, Rab7, and Rab14 have been previously shown to colocalize with bombyxin in the B. mori brain (Uno et al., ; Uno et al., ). Immunohistochemistry also revealed that Rab7 and Rab1 colocalized with eclosion hormone, while Rab1 colocalized with PTTH.…”

Section: Introductionmentioning

confidence: 96%

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Localization and functional analysis of the insect‐specific RabX4 in the brain of Bombyx mori

Uno

Furutani

Sakamoto

et al. 2017

Arch Insect Biochem Physiol

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Rab proteins are small monomeric GTPases/GTP-binding proteins, which form the largest branch of the Ras superfamily. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they function as regulators of distinct steps in membrane trafficking. RabX4 is an insect-specific Rab protein that has no close homolog in vertebrates. There is little information about insect-specific Rab proteins. RabX4 was expressed in Escherichia coli and subsequently purified. Antibodies against Bombyx mori RabX4 were produced in rabbits for western immunoblotting and immunohistochemistry. Western blotting of neural tissues revealed a single band, at approximately 26 kD. RabX4-like immunohistochemical reactivity was restricted to neurons of the pars intercerebralis and dorsolateral protocerebrum in the brain. Further immunohistochemical analysis revealed that RabX4 colocalized with Rab6 and bombyxin in the corpus allatum, a neuronal organ that secretes neuropeptides synthesized in the brain into the hemolymph. RabX4 expression in the frontal ganglion, part of the insect stomatogastric nervous system that is found in most insect orders, was restricted to two neurons on the outer region and did not colocalize with allatotropin or Rab6. Furthermore, RNA interference of RabX4 decreased bombyxin expression levels in the brain. These findings suggest that RabX4 is involved in the neurosecretion of a secretory organ in Bombyx mori.

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“…It is also a lepidopteran model organism for genetic and immunology research (Liu, Ling, & Wu, 2009;Rao et al, 2016;Wang et al, 2017). In silkworms, the Rab protein mainly functions in the development of neurons (Uno et al, 2010(Uno et al, , 2013(Uno et al, , 2014(Uno et al, , 2016(Uno et al, , 2017. However, there is no report on the role of Rab in the innate immunity of the silkworm.…”

Section: Introductionmentioning

confidence: 99%