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Your search keyword '"Roberts, Lynne"' showing total 35 results
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35 results on '"Roberts, Lynne"'

33. The Synthesis of Ricinus communis Lectins.

Author

Frigerio, Lorenzo and Roberts, Lynne M.

Abstract

Ricinus communis agglutinin II (ricin) and R. communis agglutinin I are cytotoxic seed lectins whose study has contributed to our understanding of precursor synthesis, membrane translocation, ribosome inactivation, intracellular trafficking, vacuolar targeting, protein assembly and quality control in plant cells. This chapter will focus largely on the targeting, quality control and protein assembly of these two closely related sugar binding, ribotoxic proteins. [ABSTRACT FROM AUTHOR]

Published
2010
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34. Endoplasmic Reticulum-associated Protein Degradation in Plant Cells.

Author

Robinson, David G., Ceriotti, Aldo, and Roberts, Lynne M.

Abstract

The endoplasmic reticulum (ER) is equipped with a quality control function that retains misfolded and unassembled proteins and allows only structurally mature polypeptides to be transported to their final destination. The retained proteins are eventually retro-translocated to the cytosol and destroyed by a process called endoplasmic reticulum-associated degradation (ERAD). Besides being involved in the degradation of aberrant polypeptides, the ERAD pathway is also used to regulate cellular functions and is exploited by some plant and bacterial toxins to reach the cytosol after internalization by target cells. After summarizing the general characteristics of the ERAD pathway, we describe the features of known plant ERAD substrates and of the plant degradative machinery, highlighting the role of protein disposal in the response to ER stress. [ABSTRACT FROM AUTHOR]

Published
2006
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35. Retro-Translocation of Proteins Across the Endoplasmic Reticulum Membrane.

Author

Eichler, Jerry, Lord, J. Michael, and Roberts, Lynne M.

Abstract

Many proteins synthesised in the cytosol are translocated across or inserted into the endoplasmic reticulum (ER) membrane. These proteins include not only those resident in the ER itself, but others destined for post-ER destinations such as the Golgi complex, lysosomes or secretion into the extracellular environment. Proteins that fail to fold or assemble correctly are detected by the quality control system of the ER and are disposed of by a process known as ER-associated degradation. Degradation does not occur in the ER itself. Rather the aberrant proteins are exported from the ER for degradation by the ubiquitin/proteasome pathway in the cytosol. This involves the retro-translocation of these proteins across the ER membrane. In this chapter we discuss our current understanding of the process of retro-translocation. [ABSTRACT FROM AUTHOR]

Published
2005
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