科研之友
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摘要
Extracellular proteins with important signalling roles in processes, such as inflammation and angiogenesis, are known to employ unconventional routes of protein secretion. Although mechanisms of unconventional protein secretion are beginning to emerge, the precise molecular details have remained elusive for the majority of cargo proteins secreted by unconventional means. Recent findings suggest that for two examples of unconventionally secreted proteins, interleukin 1 beta (IL-1 beta) and fibroblast growth factor 2 (FGF2), the common molecular principle of pore formation may be shared. Under specific experimental conditions, secretion of IL-1 beta and FGF2 is triggered by phosphatidylinositol 4,5-bisphosphate [PI(4,5)P-2]-dependent formation of pores across the plasma membrane. However, the underlying mechanisms are different, with FGF2 known to directly interact with PI(4,5)P-2, whereas in the case of IL-1 beta secretion, it is proposed that the N-terminal fragment of gasdermin D interacts with PI(4,5)P-2 to form the pore. Thus, although implemented in different ways, these findings suggest that pore formation may be shared by the unconventional secretion mechanisms for FGF2 and IL-1 beta in at least some cases. In this Opinion article, we discuss the unconventional mechanisms of FGF2 and IL-1 beta release with a particular emphasis on recent discoveries suggesting the importance of pore formation on the plasma membrane.
- 出版日期2017-10-1
