Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Ankyrin-B is required for intracellular sorting of structurally diverse Ca2+ homeostasis proteins
Autore:
Tuvia, S; Buhusi, M; Davis, L; Reedy, M; Bennett, V;
Indirizzi:
Duke Univ, Med Ctr, Dept Biochem, Howard Hughes Med Inst, Durham, NC 27710USA Duke Univ Durham NC USA 27710 Howard Hughes Med Inst, Durham, NC 27710USA Duke Univ, Med Ctr, Dept Cell Biol & Biochem, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 t Cell Biol & Biochem, Durham, NC 27710 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 5, volume: 147, anno: 1999,
pagine: 995 - 1007
SICI:
0021-9525(19991129)147:5<995:AIRFIS>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
T-LYMPHOMA CELLS; SARCOPLASMIC-RETICULUM; SKELETAL-MUSCLE; RYANODINE RECEPTOR; BINDING-SITES; MALIGNANT HYPERTHERMIA; ENDOPLASMIC-RETICULUM; MEMBRANE SKELETON; 440-KD ANKYRIN(B); ANION-EXCHANGER;
Keywords:
calcium homeostasis; IP3 receptor; ankyrin; sarcoplasmic reticulum; gene knockout;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Bennett, V Duke Univ, Med Ctr, Dept Biochem, Howard Hughes Med Inst, 363 Carl Bldg,Res Dr,Box 3892, Durham, NC 27710 USA Duke Univ 363 Carl Bldg,Res Dr,Box 3892 Durham NC USA 27710 USA
Citazione:
S. Tuvia et al., "Ankyrin-B is required for intracellular sorting of structurally diverse Ca2+ homeostasis proteins", J CELL BIOL, 147(5), 1999, pp. 995-1007

Abstract

This report describes a congenital myopathy and major loss of thymic lymphocytes in ankyrin-B (-/-) mice as well as dramatic alterations in intracellular localization of key components of the Ca2+ homeostasis machinery in ankyrin-B (-/-) striated muscle and thymus. The sacoplasmic reticulum (SR) and SR/T-tubule junctions are apparently preserved in a normal distribution in ankyrin-B (-/-) skeletal muscle based on electron microscopy and the presence of a normal pattern of triadin and dihydropyridine receptor, Therefore, the abnormal localization of SR/ER Ca ATPase (SERCA) and ryanodine receptors represents a defect in intracellular sorting of these proteins in skeletal muscle, Extrapolation of these observations suggests defective targeting as the basis for abnormal localization of ryanodine receptors, IP3 receptors and SERCA in heart, and of IP3 receptors in the thymus of ankyrin-B (-/-) mice. Mis-sorting of SERCA 2 and ryanodine receptor 2 in ankyrin-B (-/-)cardiomyocytes is rescued by expression of 220-kD ankyrin-B, demonstratingthat lack of the 220-kD ankyrin-B polypeptide is the primary defect in these cells. Ankyrin-B is associated with intracellular vesicles, but is not colocalized with the bulk of SERCA I or ryanodine receptor type 1 in skeletal muscle. These data provide the first evidence of a physiological requirement for ankyrin-B in intracellular targeting of the calcium homeostasis machinery of striated muscle and immune system, and moreover, support a catalytic role that does not involve permanent stoichiometric complexes between ankyrin-B and targeted proteins. Ankyrin-B is a member of a family of adapter proteins implicated in restriction of diverse proteins to specialized plasma membrane domains. Similar mechanisms involving ankyrins may be essential for segregation of functionally defined proteins within specialized regions of the plasma membrane and within the Ca2+ homeostasis compartment of the ER.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 15:06:17