Neurobiology of Disease Axonal Transport, Amyloid Precursor Protein, Kinesin-1, and the Processing Apparatus: Revisited

نویسندگان

  • Orly Lazarov
  • Gerardo A. Morfini
  • Edward B. Lee
  • Mohamed H. Farah
  • Anita Szodorai
  • Scott R. DeBoer
  • Vassilis E. Koliatsos
  • Stefan Kins
  • Virginia M.-Y. Lee
  • Philip C. Wong
  • Donald L. Price
  • Scott T. Brady
  • Sangram S. Sisodia
چکیده

Orly Lazarov,1* Gerardo A. Morfini,2* Edward B. Lee,3 Mohamed H. Farah,4 Anita Szodorai,5 Scott R. DeBoer,2 Vassilis E. Koliatsos,4 Stefan Kins,5 Virginia M.-Y. Lee,3 Philip C. Wong,4 Donald L. Price,4 Scott T. Brady,2 and Sangram S. Sisodia1 1Department of Neurobiology, Pharmacology, and Physiology, The University of Chicago, Chicago, Illinois 60637, 2Department of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612, 3Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, 4Department of Pathology, Division of Neuropathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, and 5Center of Molecular Biology Heidelberg, University of Heidelberg, D-69120 Heidelberg, Germany

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Axonal transport, amyloid precursor protein, kinesin-1, and the processing apparatus: revisited.

The sequential enzymatic actions of beta-APP cleaving enzyme 1 (BACE1), presenilins (PS), and other proteins of the gamma-secretase complex liberate beta-amyloid (Abeta) peptides from larger integral membrane proteins, termed beta-amyloid precursor proteins (APPs). Relatively little is known about the normal function(s) of APP or the neuronal compartment(s) in which APP undergoes proteolytic pr...

متن کامل

Calsyntenin-1 mediates axonal transport of the amyloid precursor protein and regulates Aβ production

Understanding the mechanisms that control processing of the amyloid precursor protein (APP) to produce amyloid-β (Aβ) peptide represents a key area of Alzheimer's disease research. Here, we show that siRNA-mediated loss of calsyntenin-1 in cultured neurons alters APP processing to increase production of Aβ. We also show that calsyntenin-1 is reduced in Alzheimer's disease brains and that the ex...

متن کامل

Loss of c-Jun N-terminal kinase-interacting protein-1 does not affect axonal transport of the amyloid precursor protein or Aβ production

Disruption to axonal transport is an early pathological feature in Alzheimer's disease. The amyloid precursor protein (APP) is a key axonal transport cargo in Alzheimer's disease since perturbation of its transport increases APP processing and production of amyloid-β peptide (Aβ) that is deposited in the brains of Alzheimer's disease patients. APP is transported anterogradely through axons on k...

متن کامل

The novel cargo Alcadein induces vesicle association of kinesin-1 motor components and activates axonal transport.

Alcadeinalpha (Alcalpha) is an evolutionarily conserved type I membrane protein expressed in neurons. We show here that Alcalpha strongly associates with kinesin light chain (K(D) approximately 4-8x10(-9) M) through a novel tryptophan- and aspartic acid-containing sequence. Alcalpha can induce kinesin-1 association with vesicles and functions as a novel cargo in axonal anterograde transport. JN...

متن کامل

Axonal Transport of Amyloid Precursor Protein Is Mediated by Direct Binding to the Kinesin Light Chain Subunit of Kinesin-I

We analyzed the mechanism of axonal transport of the amyloid precursor protein (APP), which plays a major role in the development of Alzheimer's disease. Coimmunoprecipitation, sucrose gradient, and direct in vitro binding demonstrated that APP forms a complex with the microtubule motor, conventional kinesin (kinesin-I), by binding directly to the TPR domain of the kinesin light chain (KLC) sub...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005