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Validated All-in-One™ qPCR Primer for FHOD1(NM_013241.3) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene encodes a protein which is a member of the formin/diaphanous family of proteins. The gene is ubiquitously expressed but is found in abundance in the spleen. The encoded protein has sequence homology to diaphanous and formin proteins within the Formin Homology (FH)1 and FH2 domains. It also contains a coiled-coil domain, a collagen-like domain, two nuclear localization signals, and several potential PKC and PKA phosphorylation sites. It is a predominantly cytoplasmic protein and is expressed in a variety of human cell lines. [provided by RefSeq].
Gene References into function
- FHOS mediates an interaction between GLUT4/IRAP (insulin-responsive aminopeptidase) -containing vesicles and the cytoskeleton and may participate in exocytosis and/or retention of this membrane compartment
- Fhos directly binds to F-actin via the N-terminal region, forms a homotypic complex via the FH2 domain to organize actin cytoskeleton
- FHOD1 has a role in cyclic GMP-dependent inhibition of vascular smooth muscle cell stress fiber formation and/or migration
- Oligomerization of FHOD1 via the coiled-coil motif is a critical parameter for its biological activities.
- Sustained cell elongation is a consequence of FHOD1-mediated actin-microtubule coordination.
- These novel data demonstrate that FHOD1-ERK MAP kinase interaction regulates key aspects of FHOD1 biology.
- in FHOD1, DAD acts as signal sequence for binding to the well folded and monomeric FH3 domain
- This study demonstrates FHOD1 is cleaved by caspase-3 at the SVPD(616) site during apoptosis and the C-terminal FHOD1 cleavage product has the ability to inhibit RNA polymerase I transcription.
- In this study, the N-terminal region (residues 1-339) of the human formin homology domain-containing protein 1 (FHOD1) was purified and crystallized.
- FHOD1 is activated through phosphorylation by rho-dependent protein kinase (ROCK)and has an important function in stress fibre formation in vascular endothelial cells
- The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing.
- Mutation of one residue in the predicted DAD-interaction surface efficiently activates FHOD1 in cells.