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Tctex1 overexpression promoted autophagy lysosome fusion and effectively degraded alpha-synuclein with increased cell activity
Desmosomal cadherin association with Tctex-1 and cortactin-Arp2/3 drives perijunctional actin polymerization to promote keratinocyte delamination.
results support a model in which phospho(T94)Tctex-1-regulated actin polymerization and periciliary endocytosis play an active role in orchestrating the initial phase of ciliary resorption
DYNLT1 interacts with nucleoporins and plays a role in the dysregulation of gene expression and induction of hematopoietic cell proliferation by the leukemogenic nucleoporin fusion, NUP98-HOXA9
activin receptor IIB as a novel DYNLT1 ligand and suggest that DYNLT1 functions as a molecular dimerization engine bringing together two receptor monomers in the cytoplasmic side of the membrane.
Study reports a defect in the expression of DYNLT1 in the germ cells of infertile human males and implicates DYNLT1 in spermatogonial cell division and differentiation.
The results implicate MTs/DYNLT1 as drivers of Vpr nuclear import and HIV infection, with important therapeutic implications.
Data suggest that both microtubule-associated DYNLT (dynein light chain Tctex-type 1) and cytoplasmic DYNLT (dynein 1 intermediate chain 2 DYNC1LI2) are equally able to bind to small GTPases Rab3D (Rab3d GTPase) and RagA (Ras-related GTP binding A).
Reveal a dynein independent role of Tctex-1 at the kinetochore to enhance the stability of kinetochore-microtubule attachment.
DYNLT1 is enriched at focal concentrations of CT850 on the chlamydial inclusion membrane that are known to interact with dynein and microtubules.
Data suggest that DYNLT1 phosphorylation at serine S82 is involved in microtubule and mitochondria regulation, and their interaction and cooperation contribute to the cellular hypoxic tolerance.
there are two possible mechanisms triggered by MAP4: stabilization of MT networks; DYNLT1 modulation, which is connected with VDAC1, and inhibition of hypoxia-induced mitochondrial permeabilization
Dynlt1 modulates orexin signaling by regulating OX1R
A role for Tctex-1 (DYNLT1) in controlling primary cilium length
A link between REIC/Dkk- 3 and Tctex-1 may therefore be of significance for understanding the molecular functions of the proteins in ER stress signaling and the intracellular dynein motor dynamics, respectively.
These data show that Tctex-1 may play a role in late stages of viral replication through its interaction with the flavivirus membrane protein.
Data show that Tctex-1 phosphorylated at Thr 94 is recruited to ciliary transition zones before S-phase entry and has a pivotal role in both ciliary disassembly and cell cycle progression.
Targeted disruption of Tctex-1 by RNA interference significantly impairs bone resorption capacity and mislocalizes Rab3D vesicles in osteoclasts.
These data show that both DYNLT1 and DYNLT3 interact with L2 of human papillomavirus 16 during virus infection.
The N-terminal half of pUL35, in particular residues 30-43, was identified as a common region for the binding of DYNLT1 and DYNLT3.
Cytoplasmic dynein is the major motor protein complex responsible for minus-end, microtubule-based motile processes. Each dynein complex consists of 2 heavy chains that have ATPase and motor activities, plus a group of accessory polypeptides. TCTEX1 is a dynein light chain involved in cargo binding (Chuang et al., 2005
dynein, light chain, Tctex-type 1
, dynein, light chain, Tctex-type 1 a
, t-complex testis expressed 1
, Tctex1-related dynein light chain
, dynein light chain Tctex-type 1
, T-complex testis-specific protein 1 homolog
, t-complex-associated-testis-expressed 1-like 1
, activator of G-protein signaling 2