Have you checked out SfN's eNeuro Blog? Read the newest article and let us know your thoughts!
Reviewing Editor Karl Herrup, PhD selected this paper and explains why he considers it noteworthy.
While aggregates of the microtubule associated protein tau have been associated with Alzheimer's disease (AD) since its first description, there are aspects of the tau/Alzheimer's relationship that are difficult to understand.
Tau hyper-phosphorylation facilitates its aggregation in vitro and the anatomic sites of tau aggregates correlate well with the loss of cognitive function. While these observations have held up well, it has always been a puzzle why the same post-translational phosphorylations of the tau protein that characterize the pathological aggregates found in the Alzheimer's brain are also found, without consequence, during fetal development.
Betters et al. report differences in proteins interacting with tau between fetal brain and both adult and AD brain that were not found between adult control and AD brain. Furthermore, the interaction between 14-3-3 and tau was primarily associated with 4R tau, which is lacking in fetal brain. The study does not solve the problem entirely but does offer an important advance that should be of interest to the field.
Read the full article:
Characterization of the Tau Interactome in Human Brain Reveals Isoform-Dependent Interaction with 14-3-3 Family Proteins
Ryan K. Betters, Emma Luhmann, Amy C. Gottschalk, Zhen Xu, Mallory R. Shin, Christopher P. Ptak, Kimberly L. Fiock, Lilliana C. Radoshevich, and Marco M. Hefti
Category: Editor's Pick
Tags: Disorders of the Nervous System, Neuroscience Research