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Titolo:
PHOSPHORYLATION AND SUBUNIT ORGANIZATION OF AXONAL NEUROFILAMENTS DETERMINED BY SCANNING-TRANSMISSION ELECTRON-MICROSCOPY
Autore:
LEAPMAN RD; GALLANT PE; REESE TS; ANDREWS SB;
Indirizzi:
NIH,BIOMED ENGN & INSTRUMENTAT PROGRAM,NATL CTR RES RESOURCES,BLDG 13,ROOM 3N17 BETHESDA MD 20892 NINCDS,NEUROBIOL LAB,NIH BETHESDA MD 20892
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 15, volume: 94, anno: 1997,
pagine: 7820 - 7824
SICI:
0027-8424(1997)94:15<7820:PASOOA>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENERGY-LOSS SPECTROSCOPY; EPIDERMAL KERATIN FILAMENTS; INTERMEDIATE FILAMENTS; LOSS SPECTRA; TAIL DOMAIN; ROD DOMAIN; PROTEIN; MASS; MICROANALYSIS; SPECTROMETER;
Keywords:
ELECTRON ENERGY LOSS SPECTROSCOPY; SQUID AXON; INTERMEDIATE FILAMENTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
R.D. Leapman et al., "PHOSPHORYLATION AND SUBUNIT ORGANIZATION OF AXONAL NEUROFILAMENTS DETERMINED BY SCANNING-TRANSMISSION ELECTRON-MICROSCOPY", Proceedings of the National Academy of Sciences of the United Statesof America, 94(15), 1997, pp. 7820-7824

Abstract

Phosphorylation plays a critical role in controlling the function of cytoskeletal assemblies but no direct method yet exists to measure thephosphorylation stale of proteins at the level of individual molecules and assemblies, Herein, we apply scanning transmission electron microscopy in combination with electron energy loss spectroscopy to measure the distributions of mass and phosphorus in neurofilaments (NFs) isolated from the squid giant: axon, We find that native squid NFs, in contrast to typical reconstituted intermediate filaments, are a relatively homogeneous population containing only eight coiled-foil dimers percross section, The measured stoichiometry of similar to 1:1 for light/heavy peptides strongly suggests that squid NFs are composed oi heterodimers, Furthermore, each heavy chain of the dimers carries at least 100 phosphate groups and is, therefore, near-maximally phosphorylated. These results also demonstrate that scanning transmission electron microscopy combined with electron energy loss spectroscopy at the nanometer scale is capable of characterizing the level and distribution of phosphorylation in individual mass-mapped protein assemblies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 13:04:52