Interaction of Sedlin with PAM14
- BiologyJournal of cellular biochemistry
It is suggested that nucleus‐localized Sedlin may play a role in regulation of transcriptional activities of the MRG family of transcription factors via binding to PAM14, a nuclear protein that interacts with the transcription factor MORF4‐related gene on chromosome 15 (MRG15).
Identification and Functional Analysis of SEDL-binding and Homologue Proteins by Immobilized GST Fusion and Motif Based Methods
An X-linked skeletal disorder, SEDT (spondyloepiphyseal dysplasia tarda) is a genetic disease characterized by a disproportionately short trunk and short stature caused by mutations in the SEDL gene.…
SEDLIN Forms Homodimers: Characterisation of SEDLIN Mutations and Their Interactions with Transcription Factors MBP1, PITX1 and SF1
- BiologyPloS one
Three-dimensional modelling studies of SEDLIN revealed that Asp47 resides on the surface whereas all the other mutant residues lie within the hydrophobic core of the protein, and hence are likely to affect the correct folding of S EDLIN and thereby disrupt protein-protein interactions.
CLIC4, skin homeostasis and cutaneous cancer: Surprising connections
- BiologyMolecular carcinogenesis
CLIC4 participates in normal and pathological processes and may serve as a useful target for therapies in disturbances of homeostasis and neoplastic transformation.
TRAPPC13 modulates autophagy and the response to Golgi stress
- BiologyJournal of Cell Science
The results lend support for the existence of a mammalian TRAPPIII complex containing TRAPPC13, which is important for autophagic flux under certain stress conditions.
Generation and characterization of mice with null mutation of the chloride intracellular channel 1 gene
This represents creation of the first gene knock‐out of a vertebrate CLIC protein family member and Clic1−/− mice show a mild platelet dysfunction characterized by prolonged bleeding times and decreased platelet activation in response to adenosine diphosphate stimulation linked to P2Y12 receptor signaling.
The TRAPP Complex: Insights into its Architecture and Function
- Biology, ChemistryTraffic
Recent advances in understanding of yeast and mammalian TRAPP at the structural and functional levels and its role in disease are discussed while trying to resolve some apparent discrepancies and highlighting areas for future study.
A case of spondyloepiphyseal dysplasia tarda caused by a novel intragenic deletion of TRAPPC2
- Biology, MedicineClinical pediatric endocrinology : case reports and clinical investigations : official journal of the Japanese Society for Pediatric Endocrinology
A Japanese SEDT patient is reported with a novel intragenic deletion mutation in TRAPPC2, which encodes trafficking protein particle complex subunit 2, a 140 amino acid protein, also known as Sedlin.
SHOWING 1-10 OF 21 REFERENCES
Crystal Structure of SEDL and Its Implications for a Genetic Disease Spondyloepiphyseal Dysplasia Tarda*
- BiologyThe Journal of Biological Chemistry
The 2.4 Å resolution structure of SEDL is reported, which reveals an unexpected similarity to the structures of the N-terminal regulatory domain of two SNAREs, Ykt6p and Sec22b, despite no sequence homology to these proteins.
Gene structure and expression study of the SEDL gene for spondyloepiphyseal dysplasia tarda.
It is suggested that the COOH end of the SEDL protein might be responsible for proper targeting of SEDl along the ER-Golgi membrane compartments (including Golgi and ERGIC/VTC).
Genomic structure of a novel chloride channel gene, CLIC2, in Xq28.
The NCC27 and XAP121 genes have been designated CLIC1 and CLIC2 for chloride intracellular channel genes 1 and 2, respectively since a direct association exists between a number of human chloride channel genes and a range of hereditary diseases.
TRAPP, a highly conserved novel complex on the cis‐Golgi that mediates vesicle docking and fusion
- BiologyThe EMBO journal
It is proposed that TRAPP plays a key role in the targeting and/or fusion of ER‐to‐Golgi transport vesicles with their acceptor compartment, as well as biochemical studies showing that Bet3p functions on this compartment, support this hypothesis.
Functional characterization of the NCC27 nuclear protein in stable transfected CHO‐K1 cells
- BiologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
It is demonstrated conclusively that NCC27 is a transmembrane protein that directly forms part of the ion channel and, further, that the amino terminus projects outward and the carboxyl terminus inward.
Trapp Stimulates Guanine Nucleotide Exchange on Ypt1p
- BiologyThe Journal of cell biology
These findings imply that Ypt1p, which is present on ER-to-Golgi transport vesicles, is activated at the Golgi once it interacts with TRAPP, and the purified TRAPP complex accelerates nucleotide exchange on YPT1p.
CLIC-1 functions as a chloride channel when expressed and purified from bacteria.
- BiologyThe Journal of biological chemistry
The data convincingly demonstrate that CLIC-1 is capable of forming a novel, chloride-selective channel in the absence of other subunits or proteins.
Carboxyl terminus of mitosin is sufficient to confer spindle pole localization
- BiologyJournal of cellular biochemistry
Its association with the spindle poles in normal monkey kidney CV1 cells is confirmed by indirect immunofluorescence microscopy and a possible interaction of mitosin with thespindle microtubules is suggested, implying an important role in mitosis.
The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32.
- BiologyMolecular biology of the cell
TRAPP is a large protein complex that is required for ER-to-Golgi transport and that has properties similar to those of Ypt1 GEF, andCoprecipitation and overexpression studies suggest that TRAPP can act as a GEF for Ypt 1 and Ypt31/32 in vivo.
TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport.
- Biology, ChemistryMolecular cell