Lysosomal degradation of microinjected proteins.

J. F. Dice, Hui-ling Chiang

Research output: Contribution to journalReview article

3 Citations (Scopus)

Abstract

In this article we summarize evidence for a pathway by which cytosolic proteins can be selectively taken up and degraded within lysosomes. Serum deprivation of cells in culture activates this pathway, and only proteins that contain peptide sequences related to KFERQ (lysine, phenylalanine, glutamic acid, arginine, glutamine) are degraded at enhanced rates. Approximately 30% of intracellular proteins contain such peptide sequences, and we speculate about the physiological relevance of the selective degradation of these proteins in response to serum withdrawal. Several rat tissues also contain proteins with peptide sequences related to KFERQ, and the amount of these proteins is reduced in response to starvation. Finally, we present recent results suggesting that this selective uptake of cytosolic proteins by lysosomes is not through classical macroautophagic pathways. Instead, the selective uptake may be similar to other protein sorting pathways such as protein translocation through the endoplasmic reticulum or protein import into mitochondria.

Original languageEnglish (US)
Pages (from-to)13-33
Number of pages21
JournalRevisiones sobre biologia celular : RBC
Volume20
StatePublished - 1989

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Proteolysis
Proteins
Protein Transport
Lysosomes
Peptides
Starvation
Glutamine
Serum
Phenylalanine
Endoplasmic Reticulum
Lysine
Arginine
Glutamic Acid
Mitochondria
Cell Culture Techniques

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

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title = "Lysosomal degradation of microinjected proteins.",
abstract = "In this article we summarize evidence for a pathway by which cytosolic proteins can be selectively taken up and degraded within lysosomes. Serum deprivation of cells in culture activates this pathway, and only proteins that contain peptide sequences related to KFERQ (lysine, phenylalanine, glutamic acid, arginine, glutamine) are degraded at enhanced rates. Approximately 30{\%} of intracellular proteins contain such peptide sequences, and we speculate about the physiological relevance of the selective degradation of these proteins in response to serum withdrawal. Several rat tissues also contain proteins with peptide sequences related to KFERQ, and the amount of these proteins is reduced in response to starvation. Finally, we present recent results suggesting that this selective uptake of cytosolic proteins by lysosomes is not through classical macroautophagic pathways. Instead, the selective uptake may be similar to other protein sorting pathways such as protein translocation through the endoplasmic reticulum or protein import into mitochondria.",
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Lysosomal degradation of microinjected proteins. / Dice, J. F.; Chiang, Hui-ling.

In: Revisiones sobre biologia celular : RBC, Vol. 20, 1989, p. 13-33.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Lysosomal degradation of microinjected proteins.

AU - Dice, J. F.

AU - Chiang, Hui-ling

PY - 1989

Y1 - 1989

N2 - In this article we summarize evidence for a pathway by which cytosolic proteins can be selectively taken up and degraded within lysosomes. Serum deprivation of cells in culture activates this pathway, and only proteins that contain peptide sequences related to KFERQ (lysine, phenylalanine, glutamic acid, arginine, glutamine) are degraded at enhanced rates. Approximately 30% of intracellular proteins contain such peptide sequences, and we speculate about the physiological relevance of the selective degradation of these proteins in response to serum withdrawal. Several rat tissues also contain proteins with peptide sequences related to KFERQ, and the amount of these proteins is reduced in response to starvation. Finally, we present recent results suggesting that this selective uptake of cytosolic proteins by lysosomes is not through classical macroautophagic pathways. Instead, the selective uptake may be similar to other protein sorting pathways such as protein translocation through the endoplasmic reticulum or protein import into mitochondria.

AB - In this article we summarize evidence for a pathway by which cytosolic proteins can be selectively taken up and degraded within lysosomes. Serum deprivation of cells in culture activates this pathway, and only proteins that contain peptide sequences related to KFERQ (lysine, phenylalanine, glutamic acid, arginine, glutamine) are degraded at enhanced rates. Approximately 30% of intracellular proteins contain such peptide sequences, and we speculate about the physiological relevance of the selective degradation of these proteins in response to serum withdrawal. Several rat tissues also contain proteins with peptide sequences related to KFERQ, and the amount of these proteins is reduced in response to starvation. Finally, we present recent results suggesting that this selective uptake of cytosolic proteins by lysosomes is not through classical macroautophagic pathways. Instead, the selective uptake may be similar to other protein sorting pathways such as protein translocation through the endoplasmic reticulum or protein import into mitochondria.

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