Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutanta and rescues wild-type caveolin-3. (Q42797699)

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scientific article published on December 2000

Language	Label	Description	Also known as
English	Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutanta and rescues wild-type caveolin-3.	scientific article published on December 2000

Statements

scholarly article

1 reference

Europe PubMed Central

7 November 2017

Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutanta and rescues wild-type caveolin-3. (English)

1 reference

Europe PubMed Central

7 November 2017

protein ubiquitination

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based on heuristic

inferred from title

limb-girdle muscular dystrophy

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based on heuristic

inferred from title

author name string

F Galbiati

1

1 reference

Europe PubMed Central

7 November 2017

D Volonte

2

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Europe PubMed Central

7 November 2017

C Minetti

3

1 reference

Europe PubMed Central

7 November 2017

D B Bregman

4

1 reference

Europe PubMed Central

7 November 2017

M P Lisanti

5

1 reference

Europe PubMed Central

7 November 2017

language of work or name

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publication date

1 December 2000

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Europe PubMed Central

7 November 2017

number of pages

10

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

7 November 2017

275

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Europe PubMed Central

7 November 2017

48

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Europe PubMed Central

7 November 2017

37702-37711

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Europe PubMed Central

7 November 2017

Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis

1 reference

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Molecular and cellular biology of caveolae paradoxes and plasticities.

1 reference

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Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane

1 reference

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Molecular genetics of the caveolin gene family: implications for human cancers, diabetes, Alzheimer disease, and muscular dystrophy

1 reference

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Caveolins, liquid-ordered domains, and signal transduction

1 reference

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Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts

1 reference

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The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles

1 reference

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Caveolin, a protein component of caveolae membrane coats

1 reference

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VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles

1 reference

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Identification, sequence, and expression of caveolin-2 defines a caveolin gene family

1 reference

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Caveolae and caveolins

1 reference

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Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle

1 reference

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Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo

1 reference

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Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins

1 reference

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Caveolin-3 is not an integral component of the dystrophin glycoprotein complex.

1 reference

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Oligomeric structure of caveolin: implications for caveolae membrane organization

1 reference

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Expression and Characterization of Recombinant Caveolin

1 reference

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VIP21/caveolin is a cholesterol-binding protein

1 reference

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A photo-reactive derivative of ganglioside GM1 specifically cross-links VIP21-caveolin on the cell surface.

1 reference

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Evidence for a regulated interaction between heterotrimeric G proteins and caveolin

1 reference

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Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains

1 reference

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Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases

1 reference

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Acylation targets emdothelial nitric-oxide synthase to plasmalemmal caveolae

1 reference

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Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: implications for nitric oxide signaling

1 reference

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Mutational analysis of the properties of caveolin-1. A novel role for the C-terminal domain in mediating homo-typic caveolin-caveolin interactions

1 reference

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Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells

1 reference

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Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: implications for the biogenesis of caveolae

1 reference

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Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease

1 reference

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Induction of caveolin during adipogenesis and association of GLUT4 with caveolin-rich vesicles

1 reference

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Purification and characterization of smooth muscle cell caveolae

1 reference

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Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior

1 reference

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Caveolae from luminal plasmalemma of rat lung endothelium: microdomains enriched in caveolin, Ca(2+)-ATPase, and inositol trisphosphate receptor

1 reference

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Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle

1 reference

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Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy

1 reference

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Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006657200

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Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C). Retention of LGMD-1C caveolin-3 mutants within the golgi complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006657200

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Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe

1 reference

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Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain

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UV-induced ubiquitination of RNA polymerase II: a novel modification deficient in Cockayne syndrome cells

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Ultraviolet radiation-induced ubiquitination and proteasomal degradation of the large subunit of RNA polymerase II. Implications for transcription-coupled DNA repair

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Visualization of caveolin-1, a caveolar marker protein, in living cells using green fluorescent protein (GFP) chimeras. The subcellular distribution of caveolin-1 is modulated by cell-cell contact

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Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation

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Caveolae purification and glycosylphosphatidylinositol-linked protein sorting in polarized epithelia

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Insulin stimulates the tyrosine phosphorylation of caveolin

1 reference

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Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae

1 reference

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Degradation of CFTR by the ubiquitin-proteasome pathway

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Multiple proteolytic systems, including the proteasome, contribute to CFTR processing.

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Identifiers

10.1074/JBC.M006657200

1 reference

Europe PubMed Central

7 November 2017

1 reference

Europe PubMed Central

7 November 2017

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