The transport protein particle (TRAPP) complex was initially identified as a tethering factor for COPII vesicle. Subsequently, three forms (TRAPPI, II, and III) have been found and TRAPPIII has been reported to serve as a regulator in autophagy. This study investigates a new role of mammalian TRAPPIII in ciliogenesis. We found a ciliopathy protein, oral-facial-digital syndrome 1 (OFD1), interacting with the TRAPPIII-specific subunits TRAPPC8 and TRAPPC12. TRAPPC8 is necessary for the association of OFD1 with pericentriolar material 1 (PCM1).
Trefoil Factor 1 (TFF1) belongs to the three structurally related secreted proteins that contain trefoil domains. TFF1 is an approximately 7 kDa peptide that plays an important role in epithelial regeneration and wound healing. It is highly expressed in goblet cells of the gastric and intestinal mucosa and by conjunctival goblet cells. By conserving intrachain disulfide bonds, human TFF1 formed a three-leaved conformation held together.It is a copper-binding protein that can form disulfide-linked homodimers, associate into disulfide-linked complexes with Gastrokine 2, and form non-covalent complexes with the mucin MUC5AC. TFF1 is down-regulated during the progression from gastritis to gastric dysplasia to gastric cancer, although it is up-regulated in breast and prostate cancers.
Trefoil Factor 2 (TFF2) is a member of the trefoil family and contains two P-type (trefoil) domains. Members of this family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. TFF2 is a secreted protein and specifically expressed in the stomach. TFF2 inhibits gastrointestinal motility and gastric acid secretion. TFF2 could function as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains.
Trefoil Factor 3 (TFF3) is one of three trefoil peptides secreted by epithelial cells that line mucus membranes. Trefoils contribute to protection and repair of the gastrointestinal tract. TFF3 is secreted by mucus-producing goblet cells in the large and small intestines and lower respiratory tract. It is mainly active as a disulfide-linked homodimer. The mature 59 aa, 6.5 kDa human TFF3 contains one trefoil structure formed by intramolecular disulfides and shows 76% aa identity with mouse TFF3.
TREM1 (triggering receptor expressed on myeloid cells) is a type I transmembrane protein with a single Ig-like domain; and is selectively expressed on blood neutrophils and a subset of monocytes. As a member of the growing family of receptors related to NK cell receptors; TREM1 activates downstream signaling events with the help of an adapter protein called DAP12. Expression of TREM1 is up-regulated by bacterial LPS; a ligand for TLR4; as well as lipoteichoic acid. Although its natural ligand has not been identified; engagement of TREM1 with agonist mAbs triggers secretion of the proinflammatory cytokines TNF-α and IL-1β; as well as chemokines such as IL-8 and monocyte chemoattractant protein (MCP)-1. Intracellularly; TREM1 induces Ca2+ mobilization and tyrosine phosphorylation of extracellular signal-related kinase 1 (ERK1); ERK2 and phospholipase C-γ. In an animal model of LPS-induced septic shock; blockade of TREM1 signaling inhibited hyperresponsiveness and death. Thus; it has been demonstrated that TREM1 performs a critical function in immune responses involved in host defense against microbial challenges; and is suggested to be a potential therapeutic target for septic shock.
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