Gene
Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Structure
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. 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. 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.
Function
NDEL1 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. 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. Nde1 and Ndel1 were in the past referred to as NudE and NudEL respectively. The Nde1 protein is involved in nuclear migration throughout the process of neurogenesis. Studies have revealed that Ndel1 is structurally similar to Nde1 which both play a role in microtubule-based transport. Ndel1 and Nde1 are also thought to be associated with neurodevelopmental and psychiatric disorders.
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.
Other interactions
NDEL1 has been shown to interact with Cyclin-dependent kinase 5, YWHAE, PAFAH1B1 and DISC1.
