DYNLT1

This gene encodes a component of the motor complex, cytoplasmic dynein, which transports cellular cargo along microtubules in the cell. The encoded protein regulates the length of primary cilia which are sensory organelles found on the surface of cells. The protein encoded by this gene interacts with viral proteins, like the minor capsid protein L2 of human papillomavirus, and is required for dynein-mediated delivery of the viral nucleic acid to the host nucleus. This protein interacts with oncogenic nucleoporins to disrupt gene regulation and cause leukemic transformation. Pseudogenes of this gene are present on chromosomes 4 and 17. Alternative splicing results in multiple transcript variants encoding different isoforms.

Dynein Light Chain Tctex-Type 1

Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. May also be a accessory component of axonemal dynein.

Plays a role in neuronal morphogenesis; the function is independent of cytoplasmic dynein and seems to be coupled to regulation of the actin cytoskeleton by enhancing Rac1 activity. The function in neurogenesis may be regulated by association with a G-protein beta-gamma dimer. May function as a receptor-independent activator of heterotrimeric G-protein signaling; the activation appears to be independent of a nucleotide exchange. Plays a role in regulating neurogenesis; inhibits the genesis of neurons from precursor cells during cortical development presumably by antagonizing ARHGEF2. Involved in the regulation of mitotic spindle orientation (By similarity).

Unrelated to the role in retrograde microtubule-associated movement may play a role in the dimerization of cytoplasmic proteins/domains such as for ACVR2B. Binds to the cytoplasmic domain of ACVR2B and, in vitro, inhibits ACVR2B signaling (PubMed:27502274).

(Microbial infection) Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site.

Axon development Source: Ensembl
Cell division Source: UniProtKB-KW
Dendrite development Source: Ensembl
Establishment of mitotic spindle orientation Source: UniProtKB
Intracellular transport of viral protein in host cell Source: UniProtKB
Microtubule-dependent intracellular transport of viral material towards nucleus Source: UniProtKB-KW
Negative regulation of cell death Source: Ensembl
Negative regulation of mitochondrial membrane permeability Source: Ensembl
Negative regulation of neurogenesis Source: UniProtKB
Neuron projection morphogenesis Source: Ensembl
Positive regulation of neuron projection development Source: Ensembl
Positive regulation of Rac protein signal transduction Source: Ensembl
Regulation of cytoskeleton organization Source: Ensembl
Regulation of G protein-coupled receptor signaling pathway Source: UniProtKB
Regulation of GTPase activity Source: Ensembl
Viral entry into host cell Source: UniProtKB-KW

Spindle; Golgi apparatus; Cytoplasm. Localizes to mitotic spindles.

Phosphorylated by BMPR2; the phosphorylation is abolished by BMPR2 mutations in exon 12 which lead to truncated forms of BMPR2 and which are linked to primary pulmonary hypertension (PPH1) [MIMi:178600]. The phosphorylation status is proposed to regulate the association with the cytoplasmic dynein complex and may have role in cytoplasmic dynein cargo release (By similarity).