C-terminal processing of the teneurin proteins: Independent actions of a teneurin C-terminal associated peptide in hippocampal cells

Chand, Dhan; Casatti, Cláudio Aparecido; Lannoy, Louise de; Song, Ling; Kollara, Alexandra; Baršytė-Lovejoy, Dalia; Brown, Theodore J.; Lovejoy, David A.

doi:10.1016/j.mcn.2012.09.006

Cited by 33 publications

(87 citation statements)

References 65 publications

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“…However, the promoter region for this mRNA has not been identified. In addition, immunolabelling studies performed with specific antisera indicate that the majority of the teneurin-1 immunoreactivity is confined to the plasma membrane whereas most of the TCAP-1 labeling occurs in the cytosol (Chand et al, 2012a). Taken together, this would indicate, that in some cases, TCAP-1 may be functionally independently from teneurin-1.…”

Section: Evolution and Origin Of The Teneurin C-terminal Associated Pmentioning

confidence: 93%

“…In the rodent brain, teneurin-1 (Zhou et al, 2003) and TCAP-1 (Wang et al, 2005) mRNA expression are distinct in some regions such as in the limbic areas, but overlap in others areas such as the olfactory bulb and cerebellum suggesting that the teneurin gene could be differentially regulated. In fact, northern blot studies in the adult brain and embryonic hypothalamic cell culture, demonstrated that only TCAP-1 and -3 can be independently synthesized from the larger teneurins, whereas TCAP-2 and -4 are synthesized as part of the full-length teneurin (Chand et al, 2012a;Casatti and Lovejoy, unpublished observations). Recently, we have established using 5 0 -RACE PCR, that a distinct TCAP-1 mRNA is found in mouse brain (Chand et al, 2012a).…”

Section: Evolution and Origin Of The Teneurin C-terminal Associated Pmentioning

confidence: 99%

“…In fact, northern blot studies in the adult brain and embryonic hypothalamic cell culture, demonstrated that only TCAP-1 and -3 can be independently synthesized from the larger teneurins, whereas TCAP-2 and -4 are synthesized as part of the full-length teneurin (Chand et al, 2012a;Casatti and Lovejoy, unpublished observations). Recently, we have established using 5 0 -RACE PCR, that a distinct TCAP-1 mRNA is found in mouse brain (Chand et al, 2012a). The 5 0 -untranslated region, and propeptide region are encoded within the terminal exon of the teneurin-1 gene.…”

Section: Evolution and Origin Of The Teneurin C-terminal Associated Pmentioning

confidence: 99%

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Origin of chordate peptides by horizontal protozoan gene transfer in early metazoans and protists: Evolution of the teneurin C-terminal associated peptides (TCAP)

Chand

Lannoy

Tucker

et al. 2013

General and Comparative Endocrinology

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Section: Evolution and Origin Of The Teneurin C-terminal Associated Pmentioning

confidence: 93%

Section: Evolution and Origin Of The Teneurin C-terminal Associated Pmentioning

confidence: 99%

Section: Evolution and Origin Of The Teneurin C-terminal Associated Pmentioning

confidence: 99%

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Origin of chordate peptides by horizontal protozoan gene transfer in early metazoans and protists: Evolution of the teneurin C-terminal associated peptides (TCAP)

Chand

Lannoy

Tucker

et al. 2013

General and Comparative Endocrinology

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“…Support for this proposal can be found in previous low-resolution EM images of the extracellular domains of mouse teneurin, which revealed globular domains of similar dimensions to the B/C NTR complex 18 . We predict that the YD-repeat containing domains of eukaryotic teneurins will encapsulate their carboxy-terminal regions, the teneurin carboxy-terminal associated peptides (TCAPs), which are known to be active extracellular signalling components in mice 19,20 .Previous visualisation of complete ABC Tcs from Y. entomaphaga 6 and P. luminescens 7 using EM single-particle analysis has shown that the B/C complex sits in the vestibule of the channel-forming domain of A, positioned at the end of the Tc complex furthest from the membrane.The overall shape of the B/C NTR dimer described here is consistent with the density seen in these studies 6,7 , and cross-correlation of the B/C NTR crystal structure with averaged EM projections of the Y. entomaphaga Tc (Yen-Tc) unambiguously identified the five-bladed β-propeller domain of B as the point of interaction with the A pentamer (Fig. 4a).…”

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confidence: 99%

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The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device

Busby

Panjikar

Landsberg

et al. 2013

Nature

140

198

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The ABC toxin complexes (Tc) produced by certain bacteria are of interest due to their potent insecticidal activity 1,2 and potential role in human disease 3 . These complexes comprise at least three proteins (A, B and C), which must assemble to be fully toxic 4 . The carboxy-terminal region of C is the main cytotoxic component 5 , and is poorly conserved between different Tcs. A general model of action has been proposed, in which the Tc binds to the cell surface via the A protein, is endocytosed, and subsequently forms a pH-triggered channel, allowing the translocation of C into the cytoplasm, where it can cause cytoskeletal disruption in both insect and mammalian cells 5 . Tc complexes have been visualised using single particle electron microscopy 6,7 , but no high-resolution structures of the components are available, and the role of the B protein in the mechanism of toxicity remains unknown. Here we report the three-dimensional structure of the complex formed between the B and C proteins, determined to 2.5 Å by X-ray crystallography. These proteins assemble to form an unprecedented, large hollow structure that encapsulates and sequesters the cytotoxic, carboxy-terminal region of the C protein like the shell of an egg. The shell is decorated on one end with a -propeller domain, which mediates attachment of the B/C heterodimer to the A protein in the native complex. The structure reveals how C auto-proteolyses when folded in complex with B. The C protein is the first example of a structure that contains RHS (rearrangement hot spot) repeats 8 , and illustrates a striking structural architecture that is likely conserved across both this widely distributed bacterial protein family and the related eukaryotic YD-repeatcontaining protein family, which includes the teneurins 9 . The structure provides the first clues about the function of these protein repeat families, and suggests a generic mechanism for protein encapsulation and delivery.ABC toxins were first identified, and have been best characterised, in the bacterium Photorhabdus luminescens 1 . However, the entomopathogenic bacterium Yersinia entomophaga contains a related Tc locus that includes an A component encoded by two ORFs (yenA1 and yenA2), a single B gene (yenB) and two C genes (yenC1 and yenC2), 10 the products of which associate independently with the A and B proteins, giving rise to two Tcs from one genetic locus. The C proteins of this and other Tcs are similar to the "polymorphic toxins" described by Zhang et al. 11 as they have a conserved RHS-repeat-containing amino-terminal region and a variable carboxyterminal region 10 . The carboxy-terminal regions (CTRs) of the Y. entomophaga C proteins are predicted to have different toxic activities: the C1 CTR is homologous to cytotoxic necrotising factor 1 (CNF1) from Escherichia coli 12 , whereas the C2 CTR is homologous to the deaminase YwqJ from Bacillus subtilis 13 . As in related complexes 3 , when the B subunit is co-expressed with either of the C subunits, C is cleaved at the boundary between th...

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C-terminal region of teneurin-1 co-localizes with the dystroglycan complex in adult mouse testes and regulates testicular size and testosterone production

Chand

Colacci

Dixon

et al. 2013

Histochem Cell Biol

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Testicular size is directly proportional to fertility potential and is dependent on the integration of developmental proteins, trophic factors, and sex steroids. The teneurins are transmembrane glycoproteins that function as signaling and cell adhesion molecules in the establishment and maintenance of the somatic gonad, gametogenesis, and basement membrane. Moreover, teneurins are thought to function redundantly to the extracellular matrix protein, dystroglycan. Encoded on the last exon of the teneurin genes is a family of bioactive peptides termed the teneurin C-terminal-associated peptides (TCAPs). One of these peptides, TCAP-1, functionally interacts with β-dystroglycan to act as a neuromodulatory peptide with trophic characteristics independent from the teneurins. However, little is known about the localization and relationship between the teneurin-TCAP-1 system and the dystroglycans in the gonad. In the adult mouse testis, immunoreactive TCAP-1 was localized to spermatogonia and spermatocytes and co-localized with β-dystroglycan. However, teneurin-1 was localized to the peritubular myoid cell layer of seminiferous tubules and tubules within the epididymis, and co-localized with α-dystroglycan and α-smooth muscle actin. TCAP-1-binding sites were identified in the germ cell layers and adluminal compartment of the seminiferous tubules, and epithelial cells of the epididymis. In vivo, TCAP-1 administration to adult mice for 9 days increased testicular size, seminiferous and epididymal tubule short-diameter and elevated testosterone levels. TCAP-1-treated mice also showed increased TCAP-1 immunoreactivity in the caput and corpa epididymis. Our data provide novel evidence of TCAP-1 localization in the testes that is distinct from teneurin-1, but is integrated through an association with the dystroglycan complex.

show abstract

C-terminal processing of the teneurin proteins: Independent actions of a teneurin C-terminal associated peptide in hippocampal cells

Cited by 33 publications

References 65 publications

Origin of chordate peptides by horizontal protozoan gene transfer in early metazoans and protists: Evolution of the teneurin C-terminal associated peptides (TCAP)

Origin of chordate peptides by horizontal protozoan gene transfer in early metazoans and protists: Evolution of the teneurin C-terminal associated peptides (TCAP)

The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device

C-terminal region of teneurin-1 co-localizes with the dystroglycan complex in adult mouse testes and regulates testicular size and testosterone production

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