When
cellular proteins fold improperly and clump together, they accumulate and form the plaque that is involved in the pathogenesis of Alzheimer's and other brain diseases.
As the primary site of
cellular protein folding, the ER plays a critical role in maintaining cellular function.
Not exact matches
Calcium, however, puts a strain on cells — it is known to hinder
protein -
folding and metabolism when it accumulates — disrupting normal
cellular function.
Stella M. Hurtley Senior Editor Education: B.A., University of Cambridge; Ph.D., European Molecular Biology Laboratory, Heidelberg Areas of responsibility: Cell biology,
cellular microbiology, membrane traffic,
protein targeting,
protein folding, organelle biogenesis, cytoskeleton, cell polarity, prion biology E-Mail:
[email protected]
According to a groundbreaking study published in this week's online edition of the Proceedings of the National Academy of Sciences, they have chemically synthesized a record - length mirror - image
protein and used this
protein to demonstrate that a
cellular chaperone, which helps «
fold» large or complex
proteins into their functional state, has a previously unappreciated talent — the ability to
fold mirror - image
proteins.
An additional challenge is that large
proteins often require the assistance of
cellular «chaperones» to
fold into their functional state, and D - chaperones are not available.
Once constructed, those amino acid strings spontaneously
fold up into
proteins, each with a specific 3D shape that governs its
cellular function.
During the early years of my PhD studies, I was very fascinated by the exciting discoveries in the field of signal transduction, in particular how receptor tyrosine kinases are activated to transmit their signals and how
protein complexes are formed through defined
protein folds (domains) interacting with specific
cellular targets.
However, since
folding and maintaining of such structures is highly sensitive to
cellular or environmental stress,
proteins can potentially misfold or form clumps (aggregates).
«Much work still lies ahead, but we are optimistic that the basic research toward understanding the
cellular machinery of
protein folding and quality control will eventually contribute to solving some of the most pressing medical problems of our aging population,» Hartl said.
Hartl, a biochemist, and Horwich, a geneticist, are pioneers in the realm of
cellular protein chemistry whose collaborations helped unravel the molecular machinery that assists with
protein folding.
The Kaufman lab is focused on understanding the fundamental mechanisms that regulate
protein folding and the
cellular responses to the accumulation of unfolded
proteins within the Endoplasmic Reticulum (ER).
The ER is a
cellular structure where
protein production,
folding and assembly occur.
The major portion of our research is aimed at elucidating fundamental mechanisms that regulate
protein folding and the
cellular responses to the accumulation of unfolded
protein within the (ER).
The scope of the journal encompasses all of «traditional» molecular biology (including DNA replication, recombination and repair, gene expression, RNA processing, translation, and
protein folding, modification, and degradation) as well as studies of the molecular interactions and mechanisms that underlie basic
cellular processes.
Influenza viruses can hijack host
cellular machinery to help mutated viral
proteins fold and function.
«Correct
protein folding is critically important, which is why we are focusing on the diverse set of complex
cellular mechanisms, including molecular chaperones, that promote efficient
folding and prevent toxicity,» says Dr. Adrian Israelson, who heads the
Cellular and Molecular Neurodegeneration Lab in the BGU Department of Physiology and Cell Biology.