Michael Sherman, PhD
|Institution||Boston University School of Medicine|
|Address||72 E. Concord St Silvio Conte (K)|
Boston MA 02118
|Title||Graduate Faculty (Primary Mentor of Grad Students)|
|Institution||Boston University School of Medicine, Division of Graduate Medical Sciences|
I. Research in my lab has focused on understanding the molecular mechanisms underlying the central role of the heat shock protein Hsp72 in cancer. In cancer cells Hsp72 is often expressed at very high levels, and its expression correlates with the aggressiveness of tumors. Recently we have found that Hsp72 regulates early stages of tumorigenesis. Indeed, Hsp72 can control signaling pathways initiated by major oncogenes, resulting in avoiding growth inhibition and facilitating cell proliferation and transformation.
Our research addresses several questions:
(1) How Hsp72 keeps the p53 pathway activated by PIK3CA oncogene under control?
(2) How Hsp72 prevents cell senescence activated by Her2 oncogene.
II. In a distinct project we study a process of aggregation of abnormal polypeptides. When chaperone and protein degradation machineries fail to handle abnormal proteins, they aggregate and cause cell toxicity, which may give rise to various neurological disorders. As the last line of defense, a special machinery has evolved that transports these toxic aggregates to a centrosome location via microtubules, which leads to relieve of toxicity. The resulting non-toxic single large aggregate is called aggresome. Previously we have established a yeast model to study aggregation and toxicity of the disease-causing polypeptides with expanded polyglutamine domain. Now, using both yeast and mammalian systems, we are dissecting the pathway of aggresome formation.
Our current research within this project uses genetics and biochemical approaches to addresses the following questions:
(1) What cellular components are involved in aggresome formation?
(2) What signaling pathways control aggresome formation?
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