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rh kinase and protein aggregation

Masahiko Watabe, Toshio Nakaki
Misfolded proteins are prone to form aggregates, which interfere with normal cellular functions. In general, the ubiquitin-proteasome system degrades such misfolded proteins to avoid aggregation. If this system becomes impaired or overloaded, an inclusion-body-like organelle, aggresome will operate. Misfolded protein aggregates are transported to aggresome with a deacetylase HDAC6 and dynein motors along the microtubule network, and are then removed by autophagic degradation. Although it is well known that the aggresome has evolved to cope with an excess of protein aggregates, the mechanisms underlying its formation remain unclear...
May 1, 2012: Communicative & Integrative Biology
Masahiko Watabe, Toshio Nakaki
Misfolded protein aggregates elicit a stress response, and their clearance is crucial for cell survival. These aggregates are transported by cytoplasmic deacetylase HDAC6 and dynein motors to the aggresome via the microtubule network, and are removed by autophagic degradation. HDAC6 activity is necessary for both the transport and clearance of protein aggregates. However, the cellular factors that regulate HDAC6 activity remain unknown. Here we show that protein kinase CK2 is a crucial modulator of HDAC6 activity because CK2 directly phosphorylates HDAC6 and increases cytoplasmic deacetylase activity...
May 1, 2011: Journal of Cell Science
Andrew Saxon, Daocheng Zhu, Ke Zhang, Lisa Chan Allen, Christopher L Kepley
PURPOSE OF REVIEW: This review summarizes current knowledge regarding the control of human mast cell and basophil signaling and recent developments using a new therapeutic platform consisting of a human bifunctional gamma and epsilon heavy chain (Fc gamma-Fc epsilon) protein to inhibit allergic reactivity. RECENT FINDINGS: Crosslinking of Fc gamma RIIb to Fc epsilon RI on human mast cells and basophils by a genetically engineered Fc gamma-Fc epsilon protein (GE2) leads to the inhibition of mediator release upon Fc epsilon RI challenge...
December 2004: Current Opinion in Allergy and Clinical Immunology
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