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Article: Hsp70s and lysosomal proteolysis.

Terlecky, S R

1994 Volume 50, Issue 11-12, Page(s) 1021–1025

Abstract: Confluent cultured cells activate a lysosomal pathway of polypeptide breakdown in response to withdrawal of serum growth factors. The substrates for this proteolytic pathway are a restricted class of cytosolic polypeptides containing peptide sequences ... ...

Abstract	Confluent cultured cells activate a lysosomal pathway of polypeptide breakdown in response to withdrawal of serum growth factors. The substrates for this proteolytic pathway are a restricted class of cytosolic polypeptides containing peptide sequences biochemically related to lysine-phenylalanine-glutamate-arginine-glutamine, or, in single amino acid abbreviations, KFERQ. The heat shock cognate protein of 73 kD (hsc73) binds to a variety of polypeptides via this molecular determinant and facilitates their lysosomal import and degradation. In addition, a portion of intracellular hsc73 resides within the lysosome and appears to be an essential component of the proteolytic machinery. Several potential mechanisms by which hsc73 mediates selective lysosomal import and degradation of polypeptides are discussed.
MeSH term(s)	Amino Acid Sequence ; Animals ; Biological Transport ; HSP70 Heat-Shock Proteins/physiology ; Humans ; Lysosomes/metabolism ; Molecular Sequence Data ; Oligopeptides/metabolism ; Proteins/metabolism
Chemical Substances	HSP70 Heat-Shock Proteins ; Oligopeptides ; Proteins
Language	English
Publishing date	1994-11-30
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1972-0
ISSN	0014-4754
ISSN	0014-4754
DOI	10.1007/bf01923456
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Article: How peroxisomes arise.

Terlecky, S R / Fransen, M

Traffic (Copenhagen, Denmark)

2001 Volume 1, Issue 6, Page(s) 465–473

Abstract: Peroxisomes are formed by the synthesis and assembly of membrane proteins and lipids, the selective import of proteins from the cytosol, and the growth and division of resultant organelles. To date, 23 proteins, called peroxins, are known to participate ... ...

Abstract	Peroxisomes are formed by the synthesis and assembly of membrane proteins and lipids, the selective import of proteins from the cytosol, and the growth and division of resultant organelles. To date, 23 proteins, called peroxins, are known to participate in these processes. This review summarizes recent progress in peroxin characterization and examines the underlying molecular mechanisms of peroxisome biosynthesis.
MeSH term(s)	Animals ; Biological Transport, Active ; Humans ; In Vitro Techniques ; Membrane Lipids/metabolism ; Membrane Proteins/metabolism ; Models, Biological ; Peroxisomes/metabolism ; Receptors, Cell Surface/metabolism ; Signal Transduction
Chemical Substances	Membrane Lipids ; Membrane Proteins ; Receptors, Cell Surface ; peroxisomal targeting sequence receptor
Language	English
Publishing date	2001-01-31
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1034/j.1600-0854.2000.010604.x
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Article: PTS2 protein import into mammalian peroxisomes.

Legakis, J E / Terlecky, S R

Traffic (Copenhagen, Denmark)

2001 Volume 2, Issue 4, Page(s) 252–260

Abstract: Peroxisome targeting signal (PTS)2 directs proteins from their site of synthesis in the cytosol to the lumen of the peroxisome. Unlike PTS1 which is present in the great majority of peroxisomal matrix proteins and whose import mechanics have been ... ...

Abstract	Peroxisome targeting signal (PTS)2 directs proteins from their site of synthesis in the cytosol to the lumen of the peroxisome. Unlike PTS1 which is present in the great majority of peroxisomal matrix proteins and whose import mechanics have been dissected in considerable detail, PTS2 is a relatively rare topogenic signal whose import mechanisms are far less well understood. However, as is the case for PTS1 proteins, an inability to import PTS2 proteins leads to human disease. In this report, we describe the biochemical characterization of mammalian PTS2 protein import using a semi-permeabilized cell system. We show that a PTS2-containing reporter molecule is taken up by peroxisomes in a reaction that is time-, temperature-, ATP-, and cytosol-dependent. Furthermore, the import process is specific, saturable, and requires action of the chaperone Hsc70, the cochaperone Hsp40, and the peroxins Pex5p and Pex14p. We also demonstrate peroxisomal translocation of PTS2 reporter/antibody complexes confirming the import competence of higher order structures. Importantly, cultured fibroblasts from patients with the rhizomelic form of chondrodysplasia punctata (RCDP) which are deficient for the PTS2 receptor protein, Pex7p, are unable to import the PTS2 reporter in this assay. The ability to monitor PTS2 import in vitro will permit, for the first time, a detailed comparison of the biochemical properties of PTS1 and PTS2 protein import.
MeSH term(s)	Acetyl-CoA C-Acetyltransferase/genetics ; Acetyl-CoA C-Acetyltransferase/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; CHO Cells ; Cells, Cultured ; Chondrodysplasia Punctata, Rhizomelic/genetics ; Chondrodysplasia Punctata, Rhizomelic/metabolism ; Chondrodysplasia Punctata, Rhizomelic/pathology ; Cricetinae ; Cytosol/metabolism ; Fibroblasts ; Fluorescent Antibody Technique ; HSC70 Heat-Shock Proteins ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/metabolism ; Peroxisomal Targeting Signal 2 Receptor ; Peroxisomes/metabolism ; Protein Transport ; Receptors, Cytoplasmic and Nuclear/deficiency ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Temperature ; Time Factors
Chemical Substances	DNAJB1 protein, human ; HSC70 Heat-Shock Proteins ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; HSPA8 protein, human ; Heat-Shock Proteins ; Molecular Chaperones ; Peroxisomal Targeting Signal 2 Receptor ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; Acetyl-CoA C-Acetyltransferase (EC 2.3.1.9)
Language	English
Publishing date	2001-03-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1034/j.1600-0854.2001.90165.x
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Article: Polypeptide import and degradation by isolated lysosomes.

Terlecky, S R / Dice, J F

The Journal of biological chemistry

1993 Volume 268, Issue 31, Page(s) 23490–23495

Abstract: We reported previously that lysosomes derived from human diploid fibroblasts import and degrade polypeptides and that these processes are stimulated by ATP and by the heat shock cognate protein of 73 kDa (hsc73). We now report several new aspects of this ...

Abstract	We reported previously that lysosomes derived from human diploid fibroblasts import and degrade polypeptides and that these processes are stimulated by ATP and by the heat shock cognate protein of 73 kDa (hsc73). We now report several new aspects of this in vitro proteolytic pathway. (a) Among four polypeptides tested, this pathway appears to be selective for those containing KFERQ-like peptide motifs. (b) Substrate proteins specifically bind to a protein-containing site on lysosomal membranes. (c) Lysosomes derived from serum-deprived cells are twice as active as those from serum-supplemented cells. (d) A portion of intracellular hsc73 is associated with lysosomes, and the amount of lysosomal hsc73 increases in response to serum withdrawal. Additional characterization of this proteolytic pathway not reported previously shows that intact lysosomes are required, the import process is saturable with an apparent Km of 5 microM for RNase S-peptide, and reducing agents activate this lysosomal import and degradation pathway.
MeSH term(s)	Amino Acid Sequence ; Biological Transport ; Cell Line ; Heat-Shock Proteins/metabolism ; Humans ; In Vitro Techniques ; Leupeptins/pharmacology ; Lysosomes/metabolism ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Peptides/metabolism ; Ribonuclease, Pancreatic/metabolism ; Ribonucleases/chemistry ; Ribonucleases/metabolism ; Structure-Activity Relationship
Chemical Substances	Heat-Shock Proteins ; Leupeptins ; Peptide Fragments ; Peptides ; ribonuclease S-peptide ; Ribonucleases (EC 3.1.-) ; Ribonuclease, Pancreatic (EC 3.1.27.5) ; leupeptin (J97339NR3V)
Language	English
Publishing date	1993-11-05
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article: Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import.

Fransen, M / Terlecky, S R / Subramani, S

Proceedings of the National Academy of Sciences of the United States of America

1998 Volume 95, Issue 14, Page(s) 8087–8092

Abstract: The discovery of many fatal human disorders resulting from impaired peroxisomal protein import makes the functional characterization of human peroxins critical. As part of our attempt to identify novel human genes and gene products involved in the import ...

Abstract	The discovery of many fatal human disorders resulting from impaired peroxisomal protein import makes the functional characterization of human peroxins critical. As part of our attempt to identify novel human genes and gene products involved in the import of peroxisomal proteins, we raised antisera against peroxisomal membrane proteins. One such antiserum inhibited peroxisomal protein import in semipermeabilized mammalian cells. This "import inhibiting" antiserum, ab-MF3, specifically recognized a 57-kDa protein. Immunoblot analysis of rat liver subcellular fractions demonstrated that this protein was present exclusively in peroxisomal membranes. Functional analysis revealed that this 57-kDa molecule bound the PTS1 receptor, Pex5p, in ligand blots, suggesting it is a docking site on the peroxisomal membrane. Previous studies have identified two yeast proteins, Pex14p and Pex13p, as Pex5p-binding proteins. To facilitate the biochemical analysis of peroxisomal membrane docking proteins, we cloned and expressed the previously unidentified human Pex14p, as well as a human Pex13p that is 39 aa longer than previously reported. Recombinant Pex14p was specifically recognized by the "import inhibiting" ab-MF3 and bound Pex5p and the Src homology 3 (SH3) domain of Pex13p in ligand blots. These studies demonstrate that the ab-MF3-immunoreactive, 57-kDa peroxisomal membrane protein is Pex14p. Furthermore, this peroxin interacts with Pex5p and Pex13p(SH3) and is directly required for peroxisomal protein import.
MeSH term(s)	Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport ; CHO Cells ; Cloning, Molecular ; Cricetinae ; Humans ; Ligands ; Microbodies/metabolism ; Molecular Sequence Data ; Peroxisome-Targeting Signal 1 Receptor ; Rats ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Transfection
Chemical Substances	Ligands ; Peroxisome-Targeting Signal 1 Receptor ; Receptors, Cytoplasmic and Nuclear
Language	English
Publishing date	1998-07-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.95.14.8087
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Article: Targeting of cytosolic proteins to lysosomes for degradation.

Dice, J F / Terlecky, S R

Critical reviews in therapeutic drug carrier systems

1990 Volume 7, Issue 3, Page(s) 211–233

Abstract: We review evidence for a pathway by which specific cytosolic proteins are targeted to lysosomes for degradation in cultured cells in response to serum withdrawal. This pathway is also activated by starvation in several rat tissues. The enhanced ... ...

Abstract	We review evidence for a pathway by which specific cytosolic proteins are targeted to lysosomes for degradation in cultured cells in response to serum withdrawal. This pathway is also activated by starvation in several rat tissues. The enhanced degradation is specific for a class of intracellular proteins containing peptide sequences related to residues 7 to 11 of ribonuclease A (RNase A). The amino acid sequence of this pentapeptide is lysine-phenylalanine-glutamate-arginine-glutamine, or, in single letter amino acid abbreviations, KFERQ. A heat shock protein of 73 kDa binds to such peptide regions in proteins and somehow mediates their transfer to lysosomes for degradation. The recent reconstitution of this lysosomal pathway of proteolysis in vitro should permit detailed mechanistic analysis of how proteins are directed to and translocated across lysosomal membranes.
MeSH term(s)	Animals ; Biotransformation ; Cytosol/metabolism ; Drug Carriers/metabolism ; Humans ; Lysosomes/metabolism ; Proteins/metabolism
Chemical Substances	Drug Carriers ; Proteins
Language	English
Publishing date	1990
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2012632-3
ISSN	0743-4863
ISSN	0743-4863
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Article: An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation.

Agarraberes, F A / Terlecky, S R / Dice, J F

The Journal of cell biology

1997 Volume 137, Issue 4, Page(s) 825–834

Abstract: Previous studies have implicated the heat shock cognate (hsc) protein of 73 kD (hsc73) in stimulating a lysosomal pathway of proteolysis that is selective for particular cytosolic proteins. This pathway is activated by serum deprivation in confluent ... ...

Abstract	Previous studies have implicated the heat shock cognate (hsc) protein of 73 kD (hsc73) in stimulating a lysosomal pathway of proteolysis that is selective for particular cytosolic proteins. This pathway is activated by serum deprivation in confluent cultured human fibroblasts. We now show, using indirect immunofluorescence and laser scanning confocal microscopy, that a heat shock protein (hsp) of the 70-kD family (hsp70) is associated with lysosomes (ly-hsc73). An mAb designated 13D3 specifically recognizes hsc73, and this antibody colocalizes with an antibody to lgp120, a lysosomal marker protein. Most, but not all, lysosomes contain ly-hsc73, and the morphological appearance of these organelles dramatically changes in response to serum withdrawal; the punctate lysosomes fuse to form tubules. Based on susceptibility to digestion by trypsin and by immunoblot analysis after two-dimensional electrophoresis of isolated lysosomes and isolated lysosomal membranes, most ly-hsc73 is within the lysosomal lumen. We determined the functional importance of the ly-hsc73 by radiolabeling cellular proteins with [3H]leucine and then allowing cells to endocytose excess mAb 13D3 before measuring protein degradation in the presence and absence of serum. The increased protein degradation in response to serum deprivation was completely inhibited by endocytosed mAb 13D3, while protein degradation in cells maintained in the presence of serum was unaffected. The intralysosomal digestion of endocytosed [3H]RNase A was not affected by the endocytosed mAb 13D3. These results suggest that ly-hsc73 is required for a step in the degradative pathway before protein digestion within lysosomes, most likely for the import of substrate proteins.
MeSH term(s)	Animals ; Antibodies, Monoclonal ; Antigens, CD/metabolism ; Cattle ; Cell Compartmentation ; Cells, Cultured ; Endocytosis ; Fluorescent Antibody Technique, Indirect ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Lysosomal-Associated Membrane Protein 1 ; Lysosomal Membrane Proteins ; Lysosomes/metabolism ; Membrane Glycoproteins/metabolism ; Microscopy, Confocal ; Proteins/metabolism ; Ribonuclease, Pancreatic/metabolism ; Time Factors
Chemical Substances	Antibodies, Monoclonal ; Antigens, CD ; HSP70 Heat-Shock Proteins ; Lysosomal-Associated Membrane Protein 1 ; Lysosomal Membrane Proteins ; Membrane Glycoproteins ; Proteins ; Ribonuclease, Pancreatic (EC 3.1.27.5)
Language	English
Publishing date	1997-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.137.4.825
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Article: Quantitative analysis of peroxisomal protein import in vitro.

Terlecky, S R / Legakis, J E / Hueni, S E / Subramani, S

Experimental cell research

2001 Volume 263, Issue 1, Page(s) 98–106

Abstract: Protein import into the peroxisome matrix is mediated by peroxisome-targeting signals (PTSs). We have developed a novel, quantitative, in vitro assay for measuring peroxisomal import of PTS1-containing proteins. This enzyme-linked immunosorbent assay- ... ...

Abstract	Protein import into the peroxisome matrix is mediated by peroxisome-targeting signals (PTSs). We have developed a novel, quantitative, in vitro assay for measuring peroxisomal import of PTS1-containing proteins. This enzyme-linked immunosorbent assay-based system utilizes semi-intact human A431 cells or fibroblasts and a biotinylated version of the PTS1-containing import substrate, luciferase. We show that biotinylated luciferase accumulated in peroxisomes in a time- and temperature-dependent fashion, in a reaction stimulated by exogenously added ATP, cytosol, and zinc. No import was detected in fibroblasts from a human patient belonging to complementation group 2, who suffered from the fatal peroxisomal disorder Zellweger syndrome and lacked a functional PTS1 receptor, Pex5p. Also, the reaction was significantly inhibited by antibodies to the zinc-finger protein, Pex2p. Several lines of evidence demonstrate that biotinylated luciferase was imported into the lumen of bona fide peroxisomes. (a) Biochemical fractionation of cells after the import reaction showed a time-dependent accumulation of the import substrate within intracellular organelles. (b) Confocal fluorescence microscopy indicated that imported biotinylated luciferase colocalized with the peroxisomal protein PMP70. (c) Visualization of the imported biotinylated luciferase by indirect fluorescence or indirect immunofluorescence required disruption of the peroxisomal membrane, indicating true import rather than binding to the outside of the organelle.
MeSH term(s)	Amino Acid Motifs ; Avidin/metabolism ; Biotin/metabolism ; Biotinylation ; Blotting, Western ; Cell Fractionation ; Cells, Cultured ; Conserved Sequence ; Cytoplasm/metabolism ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay/methods ; Fibroblasts ; Humans ; In Vitro Techniques ; Kinetics ; Luciferases/metabolism ; Membrane Proteins/metabolism ; Microscopy, Confocal ; Peroxisomes/chemistry ; Peroxisomes/metabolism ; Protein Transport/physiology ; Zellweger Syndrome/metabolism
Chemical Substances	Membrane Proteins ; Avidin (1405-69-2) ; Biotin (6SO6U10H04) ; Luciferases (EC 1.13.12.-)
Language	English
Publishing date	2001-02-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1006/excr.2000.5111
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Article: The cytosolic and membrane components required for peroxisomal protein import.

Terlecky, S R / Nuttley, W M / Subramani, S

Experientia

1996 Volume 52, Issue 12, Page(s) 1050–1054

Abstract: Peroxisomes are vital intracellular organelles which house enzymes involved in a variety of metabolic pathways. The large number of human disorders associated with flawed peroxisome biogenesis emphasizes the importance of protein targeting to, and ... ...

Abstract	Peroxisomes are vital intracellular organelles which house enzymes involved in a variety of metabolic pathways. The large number of human disorders associated with flawed peroxisome biogenesis emphasizes the importance of protein targeting to, and translocation across, the peroxisomal membrane. This brief review will summarize some of the emerging themes of peroxisomal protein import, specifically addressing the targeting signals possessed by constituent proteins, as well as the cytosolic, membrane and luminal components of the import machinery. Although a detailed understanding of the molecular mechanisms of peroxisomal protein import is not yet available, remarkable progress has been made in the field in recent years. An overview of these advances will be presented.
MeSH term(s)	Biological Transport ; Cell Membrane/chemistry ; Cytoplasm/chemistry ; Endoplasmic Reticulum/metabolism ; Microbodies/enzymology ; Microbodies/metabolism ; Molecular Chaperones/metabolism ; Peroxisomal Targeting Signal 2 Receptor ; Proteins/metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism
Chemical Substances	Molecular Chaperones ; Peroxisomal Targeting Signal 2 Receptor ; Proteins ; Receptors, Cytoplasmic and Nuclear
Language	English
Publishing date	1996-12-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	1972-0
ISSN	0014-4754
ISSN	0014-4754
DOI	10.1007/bf01952101
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Article: A pathway of lysosomal proteolysis mediated by the 73-kilodalton heat shock cognate protein.

Terlecky, S R / Olson, T S / Dice, J F

Acta biologica Hungarica

1991 Volume 42, Issue 1-3, Page(s) 39–47

Abstract: Cultured IMR-90 diploid human lung fibroblasts respond to withdrawal of serum or growth factors by increasing protein degradation. This increase, due to enhanced transfer of proteins into lysosomes, is specific for a class of intracellular proteins ... ...

Abstract	Cultured IMR-90 diploid human lung fibroblasts respond to withdrawal of serum or growth factors by increasing protein degradation. This increase, due to enhanced transfer of proteins into lysosomes, is specific for a class of intracellular proteins containing peptide sequences biochemically related to Lysine-Phenylalanine-Glutamate-Arginine-Glutamine (KFERQ). This peptide motif is recognized by an intracellular protein which facilitates its transfer into lysosomes in vitro and presumably, in vivo. We called this protein the peptide recognition protein of 73-kilodaltons (prp73). We have shown prp73 to be the constitutive member of the heat shock 70kD family (hsc73) by a variety of criteria. Furthermore, our reconstitution of this pathway of lysosomal degradation in vitro has provided insight in to the molecular mechanisms and requisite biochemical components.
MeSH term(s)	Amino Acid Sequence ; Cells, Cultured ; Fibroblasts/metabolism ; Heat-Shock Proteins/physiology ; Humans ; Lung/metabolism ; Lysosomes/metabolism ; Molecular Sequence Data ; Molecular Weight ; Proteins/metabolism
Chemical Substances	Heat-Shock Proteins ; Proteins ; lysosomal proteins
Language	English
Publishing date	1991
Publishing country	Hungary
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	803005-4
ISSN	1588-256X ; 0236-5383 ; 0001-5288
ISSN (online)	1588-256X
ISSN	0236-5383 ; 0001-5288
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