Study Reveals Disease-Causing Protein's Structure KIF1A-associated neurological disorders (KAND) are rare genetic conditions affecting some 580 families worldwide. These disorders are caused by mutations in the microtubule-associated motor protein KIF1A, which is essential for transporting cellular cargo along axons in neurons. Hernando J. Sosa, Ph.D., Arne Gennerich, Ph.D., and their colleagues conducted cryo-electron microscopy studies to provide the first high-resolution structure of KIF1A bound to microtubules and to identify the structural defects of the KIF1A mutant P305L, a common and devastating mutation in children with KAND. Their findings revealed that structural changes in a part of the mutated P305L protein called the K-loop prevent the KIF1A mutant from binding properly to microtubules. Their structure-function studies showed that its K-loop critically determines KIF1A’s ability to move across long distances in axons. This research suggests that the K-loop could be a therapeutic target for restoring KIF1A function in individuals with KAND. The study published online on July 2 in Nature Communications. Dr. Sosa and Dr. Gennerich are professors of biochemistry at Einstein.Posted on: Tuesday, July 02, 2024 Related News Informe de investigación Investigating a Protein's Role in Neurological Disorders Oct 03, 2023 Informe de investigación Structures of Motor Proteins Revealed Aug 23, 2022 Informe de investigación Investigating a Protein's Role in Neurological Disorders Oct 03, 2023 Comunicado de prensa For The Second Year in a Row, Two Einstein Research Teams Win Competitive XSeed Awards Mar 08, 2022
