C-terminal region of teneurin-1 co-localizes with dystroglycan and modulates cytoskeletal organization through an extracellular signal-regulated kinase-dependent stathmin- and filamin A-mediated mechanism in hippocampal cells

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

“…Immunohistochemical studies established that FITC-tagged synthetic TCAP-1 strongly co-localized with bdystroglycan at the plasma membrane. In addition, the MEK-ERK1/2 signal transduction system associated with b-dystroglycan was, likewise, stimulated by TCAP-1 and could be blocked by a MEK inhibitor (Chand et al, 2012b). Subsequently, TCAP-1 stimulated ERK1/2-dependent phosphorylation of the cytoskeleton regulatory proteins, filamin and stathmin.…”

Latrophilins updated

“…Although this assumption is tempting, it remains to be demonstrated whether this neuronal signal is actually mediated by LPHN. Additionally, the anterograde signal elicited through TEN would be a subject of great interest as it has been shown that the activation of mitogenic pathways is a part of their cellular signaling profile (79,80). Moreover, the ability of TEN to undergo proteolysis by a yet unknown mechanism and to release an intracellular domain acting on the transcriptional machinery after translocation to the nucleus interrogates if this can be modulated by their heterophilic interactions (81).…”

Teneurin C-terminal associated peptides (TCAP): modulators of corticotropin-releasing factor (CRF) physiology and behavior

“…However, in vitro screening of most of the receptors in this family did not show any significant binding or activation (Lovejoy, unpublished studies). However, gene microarray profiling indicated a similarity to neurotrophic factor activation and a relationship with the dystroglycan complex (Chand et al, 2012b). Subsequent studies confirmed this relationship, thus TCAP-1 may be the first identified soluble ligand for the dystroglycan complex.…”

“…Subsequent studies confirmed this relationship, thus TCAP-1 may be the first identified soluble ligand for the dystroglycan complex. The dystroglycan complex is hypothesized to be integral to the intracellular signaling of extracellular TCAP-1 due to a strong co-localization of TCAP-1 with β-dystroglycan, the plasma membrane bound subunit of the dystroglycan complex (Chand et al, 2012b). In essence, TCAP-1 mediates cytoskeletal re-organization in E14 cells by binding to the dystroglycan complex which then signals through a MEK- ERK1/2-dependent phosphorylation of stathmin and filamin A.…”

“…In essence, TCAP-1 mediates cytoskeletal re-organization in E14 cells by binding to the dystroglycan complex which then signals through a MEK- ERK1/2-dependent phosphorylation of stathmin and filamin A. This leads to f-actin polymerization, increased tubulin immunoreactivity, and increased filopodia development (Chand et al, 2012b). The ERK1/2 pathway is the proposed mechanism through which TCAP-1 modulates neurite and dendrite morphology in immortalized mouse hypothalamic cell lines, primary hippocampal cultures (Al Chawaf et al, 2007a), and Golgi-stained rat brains (Tan et al, 2011).…”