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Cryo-EM Structure of DPYSL2Cryo-EM Structure of DPYSL2
Structural highlights
FunctionDPYL2_BOVIN Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis (By similarity). Publication Abstract from PubMedThe use of an integrated systems biology approach to investigate tissues and organs has been thought to be impracticable in the field of structural biology, where the techniques mainly focus on determining the structure of a particular biomacromolecule of interest. Here, we report the use of cryoelectron microscopy (cryo-EM) to define the composition of a raw bovine retinal pigment epithelium (RPE) lysate. From this sample, we simultaneously identify and solve cryo-EM structures of seven different RPE enzymes whose functions affect neurotransmitter recycling, iron metabolism, gluconeogenesis, glycolysis, axonal development, and energy homeostasis. Interestingly, dysfunction of these important proteins has been directly linked to several neurodegenerative disorders, including Huntington's disease, amyotrophic lateral sclerosis (ALS), Parkinson's disease, Alzheimer's disease, and schizophrenia. Our work underscores the importance of cryo-EM in facilitating tissue and organ proteomics at the atomic level. Toward structural-omics of the bovine retinal pigment epithelium.,Morgan CE, Zhang Z, Miyagi M, Golczak M, Yu EW Cell Rep. 2022 Dec 27;41(13):111876. doi: 10.1016/j.celrep.2022.111876. PMID:36577381[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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