Abstract

Cellular life is challenged by a multitude of stress conditions, triggered for example by alterations in osmolarity, oxygen or nutrient supply. Hence, cells have developed sophisticated stress responses to cope with these challenges. Some of these stress programs such as the heat shock response are understood in great detail, while other aspects remain largely elusive including potential stress-dependent adaptations of the plasma membrane proteome. The plasma membrane is not only the first point of encounter for many types of environmental stress, but given the diversity of receptor proteins and their associated molecules also represents the site at which many cellular signal cascades originate. Since these signaling pathways affect virtually all aspects of cellular life, changes in the plasma membrane proteome appear ideally suited to contribute to the cellular adaptation to stress. The most rapid means to alter the cell surface proteome in response to stress is by alterations in endocytosis. Changes in the overall endocytic flux or in the endocytic regulation of select proteins conceivably can help to counteract adverse environmental conditions. In this review we summarize recent data regarding stress-induced changes in endocytosis and discuss how these changes might contribute to the cellular adaptation to stress in different systems. Future studies will be needed to uncover the underlying mechanisms in detail and to arrive at a coherent picture.

Highlights

  • Cells have to cope with challenging changes in their environment such as alterations in osmolarity, ion homeostasis, redox state, oxygen or nutrient supply, or exposure to ionizing radiation or potentially toxic substances

  • Deviations from homeostatic conditions are often unfavorable to cellular life and elicit stress responses that have evolved to foster adaptation to the altered conditions and, thereby, promote cellular survival in adverse environments

  • Since a number of kinases such as protein kinase N (PKN) and the mitogen-activated protein kinase (MAPK) p38 are known to be sensitive to cellular stress conditions, such as changes in osmolarity, it is conceivable how stress-induced signal cascades could lead to alterations in the uptake of specific proteins by introducing the phosphorylation of cargo or adaptor proteins

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Summary

Introduction

Cells have to cope with challenging changes in their environment such as alterations in osmolarity, ion homeostasis, redox state, oxygen or nutrient supply, or exposure to ionizing radiation or potentially toxic substances. Since a number of kinases such as protein kinase N (PKN) and the mitogen-activated protein kinase (MAPK) p38 are known to be sensitive to cellular stress conditions, such as changes in osmolarity, it is conceivable how stress-induced signal cascades could lead to alterations in the uptake of specific proteins by introducing the phosphorylation of cargo or adaptor proteins.

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