Podrobný výpis o publikaci

SKAAR, Karin, Henryj J. KORZA, Michael TARRY, Petra SEKYROVÁ a Martin HOGBOM. Expression and Subcellular Distribution of GFP-Tagged Human Tetraspanin Proteins in Saccharomyces cerevisiae. Plos one. San Francisco: Public Library of Science, 2015, roč. 10, č. 7, s. nestránkováno, 19 s. ISSN 1932-6203. Dostupné z: https://dx.doi.org/10.1371/journal.pone.0134041.

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Základní údaje
Originální název	Expression and Subcellular Distribution of GFP-Tagged Human Tetraspanin Proteins in Saccharomyces cerevisiae
Autoři	SKAAR, Karin (752 Švédsko), Henryj J. KORZA (752 Švédsko), Michael TARRY (752 Švédsko), Petra SEKYROVÁ (203 Česká republika, garant, domácí) a Martin HOGBOM (752 Švédsko).
Vydání	Plos one, San Francisco, Public Library of Science, 2015, 1932-6203.

Další údaje
Originální jazyk	angličtina
Typ výsledku	Článek v odborném periodiku
Obor	10600 1.6 Biological sciences
Stát vydavatele	Spojené státy
Utajení	není předmětem státního či obchodního tajemství
WWW	URL
Impakt faktor	Impact factor: 3.057
Kód RIV	RIV/00216224:14740/15:00087273
Organizační jednotka	Středoevropský technologický institut
Doi	http://dx.doi.org/10.1371/journal.pone.0134041
UT WoS	000358595900071
Klíčová slova anglicky	FAMILIAL EXUDATIVE VITREORETINOPATHY; EUKARYOTIC MEMBRANE-PROTEINS; ACUTE LYMPHOBLASTIC-LEUKEMIA; MALEIC ACID COPOLYMER; ENDOPLASMIC-RETICULUM; EXTRACELLULAR DOMAIN; FREE PURIFICATION; ESCHERICHIA-COLI; PICHIA-PASTORIS; QUALITY-CONTROL
Štítky	rivok
Změnil	Změnila: Mgr. Eva Špillingová, učo 110713. Změněno: 14. 4. 2016 09:19.

Anotace
Tetraspanins are integral membrane proteins that function as organizers of multimolecular complexes and modulate function of associated proteins. Mammalian genomes encode approximately 30 different members of this family and remotely related eukaryotic species also contain conserved tetraspanin homologs. Tetraspanins are involved in a number of fundamental processes such as regulation of cell migration, fusion, immunity and signaling. Moreover, they are implied in numerous pathological states including mental disorders, infectious diseases or cancer. Despite the great interest in tetraspanins, the structural and biochemical basis of their activity is still largely unknown. A major bottleneck lies in the difficulty of obtaining stable and homogeneous protein samples in large quantities. Here we report expression screening of 15 members of the human tetraspanin superfamily and successful protocols for the production in S. cerevisiae of a subset of tetraspanins involved in human cancer development. We have demonstrated the subcellular localization of overexpressed tetraspanin-green fluorescent protein fusion proteins in S. cerevisiae and found that despite being mislocalized, the fusion proteins are not degraded. The recombinantly produced tetraspanins are dispersed within the endoplasmic reticulum membranes or localized in granule-like structures in yeast cells. The recombinantly produced tetraspanins can be extracted from the membrane fraction and purified with detergents or the poly (styreneco-maleic acid) polymer technique for use in further biochemical or biophysical studies.

Anotace

Tetraspanins are integral membrane proteins that function as organizers of multimolecular complexes and modulate function of associated proteins. Mammalian genomes encode approximately 30 different members of this family and remotely related eukaryotic species also contain conserved tetraspanin homologs. Tetraspanins are involved in a number of fundamental processes such as regulation of cell migration, fusion, immunity and signaling. Moreover, they are implied in numerous pathological states including mental disorders, infectious diseases or cancer. Despite the great interest in tetraspanins, the structural and biochemical basis of their activity is still largely unknown. A major bottleneck lies in the difficulty of obtaining stable and homogeneous protein samples in large quantities. Here we report expression screening of 15 members of the human tetraspanin superfamily and successful protocols for the production in S. cerevisiae of a subset of tetraspanins involved in human cancer development. We have demonstrated the subcellular localization of overexpressed tetraspanin-green fluorescent protein fusion proteins in S. cerevisiae and found that despite being mislocalized, the fusion proteins are not degraded. The recombinantly produced tetraspanins are dispersed within the endoplasmic reticulum membranes or localized in granule-like structures in yeast cells. The recombinantly produced tetraspanins can be extracted from the membrane fraction and purified with detergents or the poly (styreneco-maleic acid) polymer technique for use in further biochemical or biophysical studies.