Functional Characterization of the Bombyx mori Fatty Acid Transport Protein (BmFATP) within the Silkmoth Pheromone Gland

Ohnishi, Atsushi; Hashimoto, Kana; Imai, Katsunori; Matsumoto, Shogo

doi:10.1074/jbc.m806072200

Cited by 54 publications

(54 citation statements)

References 33 publications

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“…Because RNAi-mediated gene silencing of BmFATP in vivo significantly suppressed LD accumulation by preventing TAG synthesis, it is obvious that BmFATP plays an essential role in LD accumulation prior to eclosion. Furthermore, in conjunction with the findings that BmFATP stimulates the uptake of extracellular LCFAs and BmFATP knockdown reduces cellular long-chain acyl-CoA synthetase activity, 47) our results indicate that BmFATP plays an essential role in pheromonogenesis by stimulating the TAG synthesis required for LD accumulation via a process similar to the so-called vectorial acylation 49) that is known to couple the uptake of extracellular fatty acids with activation to CoA thioesters.…”

Section: Fatty Acid Transport Protein (Fatp)supporting

confidence: 84%

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Molecular Mechanisms Underlying Sex Pheromone Production in Moths

Matsumoto

2010

Bioscience, Biotechnology, and Biochemistry

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Section: Fatty Acid Transport Protein (Fatp)supporting

confidence: 84%

“…Furthermore, RNAi treatment for the BmFATP gene in vivo significantly suppressed bombykol production. 47) As mentioned above, B. mori PG cells accumulate cytoplasmic LDs prior to eclosion. These LDs play a role in storing the pheromone (bombykol) precursor fatty acid in the form of TAG.…”

Section: Fatty Acid Transport Protein (Fatp)mentioning

confidence: 85%

Molecular Mechanisms Underlying Sex Pheromone Production in Moths

Matsumoto

2010

Bioscience, Biotechnology, and Biochemistry

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“…untreated controls, female moths accumulated numerous large LDs in the PG, which underwent a striking reduction after PBAN-induced LD lipolysis (Fig. 4A, a and b, also see Ohnishi et al (29)). In contrast, although RNAi-mediated knockdown of BmLsd1 had no effect on LD accumulation, PBAN-induced LD lipolysis was significantly suppressed compared with the control (Fig.…”

Section: Detection Of Pg Proteins Phosphorylated In Response To Pbanmentioning

confidence: 61%

“…3A) as well as control pupae injected with DEPC-treated H 2 O (data not shown). Although we do not know the reason for the PG-selective knockdown of BmLsd1, a similar PG-selective decrease in transcript levels was observed after knockdown of B. mori fatty acid transport protein (29) and B. mori acyl carrier protein. 5 Because BmLsd1 dsRNA injections had no effect on pupal development or adult emergence, we next injected varying concentrations (1, 5, and 10 g) of BmLsd1 dsRNA into 1-day-old female pupae.…”

Section: Detection Of Pg Proteins Phosphorylated In Response To Pbanmentioning

confidence: 72%

“…LC/MS analysis of the resulting fragment peptides generated two distinctive fragment sequences, LGTAVLDSR and SKLEVLLQQLQATSK, both of which completely matched sequences found in a B. mori cDNA clone (GenBank TM accession number DQ311207) predicted to encode perilipin. A search of the public B. mori EST data base (SilkBase) (29), which contains expressed sequence tags (EST) derived from a normalized inbred B. mori p50 strain PG cDNA library, identified a PG-expressed perilipin clone (NRPG0891).…”

Section: Detection Of Pg Proteins Phosphorylated In Response To Pbanmentioning

confidence: 99%

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Hormone Signaling Linked to Silkmoth Sex Pheromone Biosynthesis Involves Ca2+/Calmodulin-dependent Protein Kinase II-mediated Phosphorylation of the Insect PAT Family Protein Bombyx mori Lipid Storage Droplet Protein-1 (BmLsd1)

Ohnishi

Hull

Kaji

et al. 2011

Journal of Biological Chemistry

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Species-specific sex pheromones released by female moths to attract conspecific male moths are synthesized de novo in the pheromone gland (PG) via the fatty acid biosynthetic pathway. This pathway is regulated by a neurohormone termed pheromone biosynthesis activating neuropeptide (PBAN), a 33-amino acid peptide that originates in the subesophageal ganglion. In the silkmoth, Bombyx mori, cytoplasmic lipid droplets, which store the sex pheromone (bombykol) precursor fatty acid, accumulate in PG cells. PBAN stimulates lipolysis of the stored lipid droplet triacylglycerols (TAGs) and releases the precursor for final modification. PBAN exerts its physiological function via the PG cell-surface PBAN receptor, a G protein-coupled receptor that belongs to the neuromedin U receptor family. The PBAN receptor-mediated signal is transmitted via a canonical store-operated channel activation pathway utilizing Gq-medi- Mating in moths is limited to a specific phase of the photoperiod and developmental stage. Accordingly, the biochemical processes that comprise sex pheromone biosynthesis in female moths must be precisely regulated. In most moth species these processes are regulated by a neurohormone termed pheromone biosynthesis activating neuropeptide (PBAN), 4 a 33-amino acid peptide that originates in the subesophageal ganglion and that is characterized by a core C-terminal FSPRLamide sequence (1, 2). After adult emergence, PBAN is released into the hemolymph during a species-specific period and acts on the pheromone gland (PG) to trigger the production and release of species-specific sex pheromones (3, 4).PG is a functionally differentiated organ in close proximity to the terminal abdominal tip that originates in the intersegmental membrane between the 8th and 9th abdominal segments (5-7). In the silkmoth, Bombyx mori, the sex pheromone, E,Z-10,12-hexadecadien-1-ol, commonly known as bombykol, is synthesized de novo within PG cells from acetyl-CoA via the conventional long chain fatty acid biosynthetic pathway (8, 9). The straight chain fatty acyl intermediate, palmitate, is converted stepwise to bombykol by the actions of a bifunctional Z11-10/12 fatty acyl desaturase, Bmpgdesat1, and a PG-specific fatty acyl reductase, pgFAR (10 -12). On the day before adult emergence, B. mori PG cells rapidly accumulate numerous lipid droplets (LDs) within the cytoplasm (13). These LDs play an essential role in bombykol biosynthesis by acting as a reservoir for the de novo synthesized bombykol precursor, ⌬10,12-hexadecadienoate, which is deposited in the LDs in the form of triacylglycerols (TAGs) with the precursor predominantly sequestered at the sn-1 and sn-3 positions of the glycerides (14). After adult emergence, the stored fatty acid is cleaved and converted to bombykol in response to PBAN (7,15).The pheromonotropic effects of PBAN are dependent on extracellular Ca 2ϩ (3,4) and are mediated by the PG cell-surface PBAN receptor, a G protein-coupled receptor that belongs to the neuromedin U receptor family (16 -18

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A journey into the world of insect lipid metabolism

Toprak¹,

Hegedus

Doğan³

et al. 2020

Arch Insect Biochem Physiol

124

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Lipid metabolism is fundamental to life. In insects, it is critical, during reproduction, flight, starvation, and diapause. The coordination center for insect lipid metabolism is the fat body, which is analogous to the vertebrate adipose tissue and liver. Fat body contains various different cell types; however, adipocytes and oenocytes are the primary cells related to lipid metabolism. Lipid metabolism starts with the hydrolysis of dietary lipids, absorption of lipid monomers, followed by lipid transport from midgut to the fat body, lipogenesis or lipolysis in the fat body, and lipid transport from fat body to other sites demanding energy. Lipid metabolism is under the control of hormones, transcription factors, secondary messengers and posttranscriptional modifications. Primarily, lipogenesis is under the control of insulin‐like peptides that activate lipogenic transcription factors, such as sterol regulatory element‐binding proteins, whereas lipolysis is coordinated by the adipokinetic hormone that activates lipolytic transcription factors, such as forkhead box class O and cAMP‐response element‐binding protein. Calcium is the primary–secondary messenger affecting lipid metabolism and has different outcomes depending on the site of lipogenesis or lipolysis. Phosphorylation is central to lipid metabolism and multiple phosphorylases are involved in lipid accumulation or hydrolysis. Although most of the knowledge of insect lipid metabolism comes from the studies on the model Drosophila; other insects, in particular those with obligatory or facultative diapause, also have great potential to study lipid metabolism. The use of these models would significantly improve our knowledge of insect lipid metabolism.

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Functional Characterization of the Bombyx mori Fatty Acid Transport Protein (BmFATP) within the Silkmoth Pheromone Gland

Cited by 54 publications

References 33 publications

Molecular Mechanisms Underlying Sex Pheromone Production in Moths

Molecular Mechanisms Underlying Sex Pheromone Production in Moths

Hormone Signaling Linked to Silkmoth Sex Pheromone Biosynthesis Involves Ca2+/Calmodulin-dependent Protein Kinase II-mediated Phosphorylation of the Insect PAT Family Protein Bombyx mori Lipid Storage Droplet Protein-1 (BmLsd1)

A journey into the world of insect lipid metabolism

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