2024年12月24日 · DYNLL1 (Dynein Light Chain LC8-Type 1) is a Protein Coding gene. Diseases associated with DYNLL1 include Rabies and Lissencephaly 1. Among its related pathways are Loss of proteins required for interphase microtubule organization from the centrosome and EML4 and NUDC in mitotic spindle formation.

Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility.

2018年10月31日 · In cells, DYNLL1 limits nucleolytic degradation of DNA ends by associating with the DNA end-resection machinery (MRN complex, BLM helicase and DNA2 endonuclease). In vitro, DYNLL1 binds...

Dynein light chain LC8 alleviates nonalcoholic steatohepatitis by inhibiting NF-kappaB signaling and reducing oxidative stress. DYNLL1 is hypomethylated and upregulated in a tumor stage- and grade-dependent manner and associated with increased mortality in hepatocellular carcinoma.

细胞质动力蛋白是分子量约为 1,200 kD 的大型酶复合物。 它们包含两个主要由动力蛋白重链形成的力产生头，以及将头连接到基底域的茎，基底域包含数量不等的辅助中间链。 该复合物参与细胞内运输和运动。 该记录中描述的蛋白质是一条轻链，作为该复合物的一部分存在，但也与神经元一氧化氮合酶发生物理相互作用并抑制其活性。 这种蛋白质的结合使神经元一氧化氮合酶二聚体不稳定，这是一种活动所必需的构象，并且它可以通过其对一氧化氮合酶活性的影响来调节许多生 …

2024年1月4日 · 摘要：dynll1蛋白是一种重要的动力蛋白轻链，参与细胞运动、形态变化和细胞器的定位等生物学过程。 它能够调控微管的聚合和解聚，影响细胞定位运动、分裂和迁移等。

2023年9月11日 · Here we describe how the 53BP1-associated protein DYNLL1 works in tandem with the Shieldin complex to protect DNA ends. DYNLL1 is recruited to DSBs by 53BP1, where it limits end resection by...

2019年4月22日 · To define the contribution of the LC8-type dynein light chain subunit to the CD2 complex, we have generated Dynll1 -deficient mouse strains, including the first-ever conditional knockout (KO) mutant for any CD2 subunit. Germline Dynll1 KO mice exhibit a severe ciliopathy-like phenotype similar to mice lacking another CD2 subunit, Dync2li1.

2020年11月8日 · In cells, DYNLL1 limits nucleolytic degradation of DNA ends by associating with the DNA end-resection machinery (MRN complex, BLM helicase and DNA2 endonuclease). In vitro, DYNLL1 binds directly to MRE11 to limit its end-resection activity.

DLC 1 (also known as DYNLL1, LC8, and PIN) is ubiquitously expressed and participates in a variety of essential intracellular events. DLC1 transition from monomer to dimer is crucial for its function, and this process is regulated by p21-activated kinase 1 (Pak1) phosphorylation of Ser88 in DLC1 [66,67].