NDEL1
Protein-coding gene in the species Homo sapiens
From Wikipedia, the free encyclopedia
Nuclear distribution protein nudE-like 1 is a protein that in humans is encoded by the NDEL1 gene.[5][6][7]
It plays a significant role in intracellular transport and the process of cellular division via regulation of the dynein motor protein and its cofactor protein, Lis1.[8] Ndel1 is a highly conserved protein and its human gene, NDEL1 is expressed in a wide variety of brain tissues which contributes to neuronal function and development.[9][10][11] Nde1 and Ndel1 were in the past referred to as NudE and NudEL respectively.[12][13] The Nde1 protein is involved in nuclear migration throughout the process of neurogenesis.[14] Studies have revealed that Ndel1 is structurally similar to Nde1 which both play a role in microtubule-based transport.[8] Ndel1 and Nde1 are also thought to be associated with neurodevelopmental and psychiatric disorders.[14][15] Secondary structure of Ndel1 is composed of various distinct domains: a C-terminal region, and a 200 amino acid N-terminal coiled-coil domain. The coiled-coil domain of Ndel1 serves as a self-associating stable parallel homodimer.[16] Such structural components help with interactions between an array of binding partners, including the motor protein dynein and its cofactor protein, Lis1. Ndel1 forms a heterotetramer complex with Lis1 via the N-terminal coiled-coil domain.[16] The Ndel1 N-terminal coiled-coil domain mediates binding to dynein, whereas the C-terminal domain interacts with Lis1, regulating the activity of the dynein complex.[13]
This gene product is a thiol-activated oligopeptidase and is also known as Endooligopeptidase A in that context. It is phosphorylated in M phase of the cell cycle. Phosphorylation regulates the cell cycle-dependent distribution of this protein, with a fraction of the protein bound strongly to centrosomes in interphase and localized to mitotic spindles in early M phase. Overall, this protein plays a role in nervous system development. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[7]