Dd-TRAP1 is a Dictyostelium homologue of TRAP-1, a human protein that binds to the type 1 tumor necrosis factor (TNF) receptor. TRAP-1 has a putative mitochondrial localization sequence and shows significant homology to members of the HSP90 family. Although TRAP-1 is mainly localized to mitochondria in several mammalian cells, in certain tissues it is also localized at specific extramitochondrial sites. In Dictyostelium cells, Dd-TRAP1 is predominantly located in the cell membrane/cortex during growth and just after starvation. Double staining of vegetatively growing cells with the anti-Dd-TRAP1 antibody and TRITC-phalloidin has demonstrated colocalization of Dd-TRAP1 and F-actin at the leading edge of cortical protrusions such as pseudopodes. Coupled with differentiation, however, Dd-TRAP1 located at the cortical region is translocated to mitochondria in spite of the absence of the mitochondrial localization sequence at its N-terminus. The translocation of this protein raises interesting and fundamental questions regarding possible mechanisms by which Dd-TRAP1 is involved in cellular differentiation.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1006/excr.2002.5620 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Cross-Species Applications of Peptide Substrate Reporters to Quantitative Measurements of Kinase Activity.
ACS Meas Sci Au
October 2024
Department of Chemistry, Trinity College, 300 Summit St., Hartford, Connecticut 06106, United States.
Peptide substrate reporters are short chains of amino acids designed to act as substrates for enzymes of interest. Combined with capillary electrophoresis and laser-induced fluorescence detection (CE-LIF), they are powerful molecular tools for quantitative measurements of enzyme activity even at the level of single cells. Although most peptide substrate reporters have been optimized for human or murine cells in health-related applications, their performance in nonmammalian organisms remains largely unexplored.
View Article and Find Full Text PDFPolycystin-2 Mediated Calcium Signalling in the Model for Autosomal Dominant Polycystic Kidney Disease.
Cells
March 2024
Department of Microbiology, Anatomy, Physiology and Pharmacology, La Trobe University, Bundoora, Melbourne, VIC 3086, Australia.
Autosomal dominant polycystic kidney disease (ADPKD) occurs when the proteins Polycystin-1 (PC1, ) and Polycystin-2 (PC2, ) contain mutations. PC1 is a large membrane receptor that can interact and form a complex with the calcium-permeable cation channel PC2. This complex localizes to the plasma membrane, primary cilia and ER.
View Article and Find Full Text PDFReduced PaxillinB localization to cell-substrate adhesions promotes cell migration in .
bioRxiv
March 2024
Department of Biochemistry, University of Utah, Salt Lake City, UT, 84112, USA.
Many cells adhere to extracellular matrix for efficient cell migration. This adhesion is mediated by focal adhesions, a protein complex linking the extracellular matrix to the intracellular cytoskeleton. Focal adhesions have been studied extensively in mesenchymal cells, but recent research in physiological contexts and amoeboid cells suggest focal adhesion regulation differs from the mesenchymal focal adhesion paradigm.
View Article and Find Full Text PDFAn evolutionarily conserved bimodular domain anchors ZC3HC1 and its yeast homologue Pml39p to the nuclear basket.
Mol Biol Cell
May 2023
Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany.
The proteins ZC3HC1 and TPR are structural components of the nuclear basket (NB), a fibrillar structure attached to the nucleoplasmic side of the nuclear pore complex (NPC). ZC3HC1 initially binds to the NB in a TPR-dependent manner and can subsequently recruit additional TPR polypeptides to this structure. Here, we examined the molecular properties of ZC3HC1 that enable its initial binding to the NB and TPR.
View Article and Find Full Text PDFThe Model for Mucolipidosis Type IV.
Front Cell Dev Biol
April 2022
Department of Physiology, Anatomy and Microbiology, La Trobe University, Melbourne, VIC, Australia.
Mucolipidosis type IV, a devastating neurological lysosomal disease linked to mutations in the transient receptor potential channel mucolipin 1, TRPML1, a calcium permeable channel in the membranes of vesicles in endolysosomal system. TRPML1 function is still being elucidated and a better understanding of the molecular pathogenesis of Mucolipidosis type IV, may facilitate development of potential treatments. We have created a model to study mucolipin function in the eukaryotic slime mould by altering expression of its single mucolipin homologue, .
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!