• Je něco špatně v tomto záznamu ?

The role of palmitoylation and transmembrane domain in sorting of transmembrane adaptor proteins

T. Chum, D. Glatzová, Z. Kvíčalová, J. Malínský, T. Brdička, M. Cebecauer,

. 2016 ; 129 (1) : 95-107. [pub] 20151119

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc17000861

Plasma membrane proteins synthesised at the endoplasmic reticulum are delivered to the cell surface via sorting pathways. Hydrophobic mismatch theory based on the length of the transmembrane domain (TMD) dominates discussion about determinants required for protein sorting to the plasma membrane. Transmembrane adaptor proteins (TRAP) are involved in signalling events which take place at the plasma membrane. Members of this protein family have TMDs of varying length. We were interested in whether palmitoylation or other motifs contribute to the effective sorting of TRAP proteins. We found that palmitoylation is essential for some, but not all, TRAP proteins independent of their TMD length. We also provide evidence that palmitoylation and proximal sequences can modulate sorting of artificial proteins with TMDs of suboptimal length. Our observations point to a unique character of each TMD defined by its primary amino acid sequence and its impact on membrane protein localisation. We conclude that, in addition to the TMD length, secondary sorting determinants such as palmitoylation or flanking sequences have evolved for the localisation of membrane proteins.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc17000861
003      
CZ-PrNML
005      
20170118124217.0
007      
ta
008      
170103s2016 enk f 000 0|eng||
009      
AR
024    7_
$a 10.1242/jcs.175190 $2 doi
024    7_
$a 10.1242/jcs.175190 $2 doi
035    __
$a (PubMed)26585312
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a enk
100    1_
$a Chum, Tomáš $u Department of Biophysical Chemistry, J. Heyrovsky Institute of Physical Chemistry, Czech Academy of Sciences, Dolejskova 3, 18223 Prague, Czech Republic.
245    14
$a The role of palmitoylation and transmembrane domain in sorting of transmembrane adaptor proteins / $c T. Chum, D. Glatzová, Z. Kvíčalová, J. Malínský, T. Brdička, M. Cebecauer,
520    9_
$a Plasma membrane proteins synthesised at the endoplasmic reticulum are delivered to the cell surface via sorting pathways. Hydrophobic mismatch theory based on the length of the transmembrane domain (TMD) dominates discussion about determinants required for protein sorting to the plasma membrane. Transmembrane adaptor proteins (TRAP) are involved in signalling events which take place at the plasma membrane. Members of this protein family have TMDs of varying length. We were interested in whether palmitoylation or other motifs contribute to the effective sorting of TRAP proteins. We found that palmitoylation is essential for some, but not all, TRAP proteins independent of their TMD length. We also provide evidence that palmitoylation and proximal sequences can modulate sorting of artificial proteins with TMDs of suboptimal length. Our observations point to a unique character of each TMD defined by its primary amino acid sequence and its impact on membrane protein localisation. We conclude that, in addition to the TMD length, secondary sorting determinants such as palmitoylation or flanking sequences have evolved for the localisation of membrane proteins.
650    _2
$a adaptorové proteiny signální transdukční $x chemie $x metabolismus $7 D048868
650    _2
$a buněčná membrána $x metabolismus $7 D002462
650    _2
$a extracelulární prostor $x chemie $7 D005110
650    _2
$a glykosylace $7 D006031
650    _2
$a HEK293 buňky $7 D057809
650    _2
$a HeLa buňky $7 D006367
650    _2
$a lidé $7 D006801
650    _2
$a Jurkat buňky $7 D019169
650    12
$a lipoylace $7 D054878
650    _2
$a membránové proteiny $x chemie $x metabolismus $7 D008565
650    _2
$a terciární struktura proteinů $7 D017434
650    _2
$a transport proteinů $7 D021381
650    _2
$a vztahy mezi strukturou a aktivitou $7 D013329
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Glatzová, Daniela $u Department of Biophysical Chemistry, J. Heyrovsky Institute of Physical Chemistry, Czech Academy of Sciences, Dolejskova 3, 18223 Prague, Czech Republic Laboratory of Leukocyte Signaling, Institute of Molecule Genetics, Czech Academy of Sciences, Videnska 1083, Prague, Czech Republic.
700    1_
$a Kvíčalová, Zuzana $u Department of Biophysical Chemistry, J. Heyrovsky Institute of Physical Chemistry, Czech Academy of Sciences, Dolejskova 3, 18223 Prague, Czech Republic.
700    1_
$a Malínský, Jan $u Microscopy Unit, Institute of Experimental Medicine, Czech Academy of Sciences, Videnska 1083, 14220 Prague, Czech Republic.
700    1_
$a Brdička, Tomáš $u Laboratory of Leukocyte Signaling, Institute of Molecule Genetics, Czech Academy of Sciences, Videnska 1083, Prague, Czech Republic.
700    1_
$a Cebecauer, Marek $u Department of Biophysical Chemistry, J. Heyrovsky Institute of Physical Chemistry, Czech Academy of Sciences, Dolejskova 3, 18223 Prague, Czech Republic marek.cebecauer@jh-inst.cas.cz.
773    0_
$w MED00002576 $t Journal of cell science $x 1477-9137 $g Roč. 129, č. 1 (2016), s. 95-107
856    41
$u https://pubmed.ncbi.nlm.nih.gov/26585312 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20170103 $b ABA008
991    __
$a 20170118124323 $b ABA008
999    __
$a ok $b bmc $g 1180001 $s 961428
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2016 $b 129 $c 1 $d 95-107 $e 20151119 $i 1477-9137 $m Journal of cell science $n J Cell Sci $x MED00002576
LZP    __
$a Pubmed-20170103

Najít záznam

Citační ukazatele

Možnosti archivace