Two major cuticular proteins are required for assembly of horizontal laminae and vertical pore canals in rigid cuticle of Tribolium castaneum

Noh, Mi Young; Kramer, Karl J.; Muthukrishnan, Subbaratnam; Kanost, Michael R.; Beeman, Richard W.; Arakane, Yasuyuki

doi:10.1016/j.ibmb.2014.07.005

Cited by 90 publications

(97 citation statements)

References 34 publications

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“…8). All insects establish compact and structured exoskeletal cuticles at their outermost body parts (4,29,32,33,36,37). Our data argue that structural similarities of the body wall cuticle and molecular conservation of involved proteins (8, 9, 15-19, 38 -40) point toward a highly conserved mechanism of procuticle formation among chitinous invertebrates.…”

Section: Discussionmentioning

confidence: 70%

Obstructor A Organizes Matrix Assembly at the Apical Cell Surface to Promote Enzymatic Cuticle Maturation in Drosophila

Pesch

Riedel

Behr

2015

Journal of Biological Chemistry

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Background:The apical extracellular matrix (aECM) protects against environmental stresses that attack organisms throughout lifetime. Results: Epidermal cells secrete obstructor A into a core organizer region for controlling aECM assembly at the apical cell surface. Conclusion: Normal aECM assembly is mediated by obstructor A and regulates cuticle stability at the epidermis. Significance: Cuticle formation of the insect epidermis is genetically conserved.

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Section: Discussionmentioning

confidence: 70%

Obstructor A Organizes Matrix Assembly at the Apical Cell Surface to Promote Enzymatic Cuticle Maturation in Drosophila

Pesch

Riedel

Behr

2015

Journal of Biological Chemistry

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“…EM immunolocalization of an RR-2 protein from Tribolium castaneum (TcCPR27) localized it in both laminae and vertical pore canals of the elytra’s hard cuticle (Noh et al, 2014). Since only cuticle from pharate adults was examined, no information is available about whether this protein might also be found in the post-ecdysial endocuticle.…”

Section: Introductionmentioning

confidence: 99%

Localization of RR-1 and RR-2 cuticular proteins within the cuticle of Anopheles gambiae

Vannini

Willis

2017

Arthropod Structure & Development

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The largest arthropod cuticular protein family, CPR, has the Rebers and Riddiford (R&R) Consensus that in an extended form confers chitin-binding properties. Two forms of the Consensus, RR-1 and RR-2, have been recognized and initial data suggested that the RR-1 and RR-2 proteins were present in different regions within the cuticle itself. Thus, RR-2 proteins would contribute to exocuticle that becomes sclerotized, while RR-1s would be found in endocuticle that remains soft. An alternative, and more common, suggestion is that RR-1 proteins are used for soft, flexible cuticles such as intersegmental membranes, while RR-2s are associated with hard cuticle such as sclerites and head capsules. We used TEM immunogold detection to localize the position of several RR-1 and RR-2 proteins in the cuticle of Anopheles gambiae. RR-1s were localized in the procuticle of the soft intersegmental membrane except for one protein found in the endocuticle of hard cuticle. RR-2s were consistently found in hard cuticle and not in flexible cuticle. All RR-2 antibodies localized to the exocuticle and four out of six were also found in the endocuticle. Hence the location of RR-1s and RR-2s depends more on properties of individual proteins than on either hypothesis.

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“…Given the large number of structural cuticular proteins, one might expect that there would be proteins playing unique roles in specific structures. Indeed, recent analyses in Tribolium castaneum focused on just three proteins found, but not exclusively, in the elytra and demonstrated essential roles for each (Arakane et al, 2012; Noh et al, 2014, 2015). …”

Section: Introductionmentioning

confidence: 99%

Distribution of cuticular proteins in different structures of adult Anopheles gambiae

Zhou

Badgett

Bowen

et al. 2016

Insect Biochemistry and Molecular Biology

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Anopheles gambiae devotes over 2% (295) of its protein coding genes to structural cuticular proteins (CPs) that have been classified into 13 different families plus ten low complexity proteins not assigned to families. Small groups of genes code for identical proteins reducing the total number of unique cuticular proteins to 282. Is the large number because different structures utilize different CPs, or are all of the genes widely expressed? We used LC-MS/MS to learn how many products of these genes were found in five adult structures: Johnston's organs, the remainder of the male antennae, eye lenses, legs, and wings. Data were analyzed against both the entire proteome and a smaller database of just CPs. We recovered unique peptides for 97 CPs and shared peptides for another 35. Members of 11 of the 13 families were recovered as well as some unclassified. Only 11 CPs were present exclusively in only one structure while 43 CPs were recovered from all five structures. A quantitative analysis, using normalized spectral counts, revealed that only a few CPs were abundant in each structure. When the MS/MS data were run against the entire proteome, the majority of the top hits were to CPs, but peptides were recovered from an additional 467 proteins. CP peptides were frequently recovered from chitin-binding domains, confirming that protein-chitin interactions are not mediated by covalent bonds. Comparison with three other MS/MS analyses of cuticles or cuticle-rich structures augmented the current analysis. Our findings provide new insights into the composition of different mosquito structures and reveal the complexity of selection and utilization of genes coding for structural cuticular proteins.

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Two major cuticular proteins are required for assembly of horizontal laminae and vertical pore canals in rigid cuticle of Tribolium castaneum

Cited by 90 publications

References 34 publications

Obstructor A Organizes Matrix Assembly at the Apical Cell Surface to Promote Enzymatic Cuticle Maturation in Drosophila

Obstructor A Organizes Matrix Assembly at the Apical Cell Surface to Promote Enzymatic Cuticle Maturation in Drosophila

Localization of RR-1 and RR-2 cuticular proteins within the cuticle of Anopheles gambiae

Distribution of cuticular proteins in different structures of adult Anopheles gambiae

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