-
Something wrong with this record ?
LST1/A is a myeloid leukocyte-specific transmembrane adaptor protein recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to the plasma membrane
P. Draber, O. Stepanek, M. Hrdinka, A. Drobek, L. Chmatal, L. Mala, T. Ormsby, P. Angelisova, V. Horejsi, T. Brdicka
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 2008 to 1 year ago
Freely Accessible Science Journals
from 1905 to 1 year ago
PubMed Central
from 2005
Europe PubMed Central
from 2005 to 1 year ago
Open Access Digital Library
from 1905-10-01
Open Access Digital Library
from 1905-10-01
ROAD: Directory of Open Access Scholarly Resources
from 1905
- MeSH
- Cell Membrane metabolism MeSH
- HEK293 Cells MeSH
- HeLa Cells MeSH
- Major Histocompatibility Complex physiology MeSH
- Jurkat Cells MeSH
- Humans MeSH
- Membrane Proteins chemistry genetics metabolism MeSH
- Molecular Sequence Data MeSH
- Myeloid Cells cytology metabolism MeSH
- Plakins metabolism MeSH
- Primary Cell Culture MeSH
- Pseudopodia metabolism MeSH
- Amino Acid Sequence MeSH
- Signal Transduction physiology MeSH
- Protein Structure, Tertiary physiology MeSH
- Protein Transport physiology MeSH
- Protein Tyrosine Phosphatase, Non-Receptor Type 11 metabolism MeSH
- Protein Tyrosine Phosphatase, Non-Receptor Type 6 metabolism MeSH
- U937 Cells MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Transmembrane adaptor proteins are membrane-anchored proteins consisting of a short extracellular part, a transmembrane domain, and a cytoplasmic part with various protein-protein interaction motifs but lacking any enzymatic activity. They participate in the regulation of various signaling pathways by recruiting other proteins to the proximity of cellular membranes where the signaling is often initiated and propagated. In this work, we show that LST1/A, an incompletely characterized protein encoded by MHCIII locus, is a palmitoylated transmembrane adaptor protein. It is expressed specifically in leukocytes of the myeloid lineage, where it localizes to the tetraspanin-enriched microdomains. In addition, it binds SHP-1 and SHP-2 phosphatases in a phosphotyrosine-dependent manner, facilitating their recruitment to the plasma membrane. These data suggest a role for LST1/A in negative regulation of signal propagation.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc12034503
- 003
- CZ-PrNML
- 005
- 20170131075203.0
- 007
- ta
- 008
- 121023s2012 xxu f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1074/jbc.m112.339143 $2 doi
- 035 __
- $a (PubMed)22589543
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Dráber, Peter $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic $7 xx0140504
- 245 10
- $a LST1/A is a myeloid leukocyte-specific transmembrane adaptor protein recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to the plasma membrane / $c P. Draber, O. Stepanek, M. Hrdinka, A. Drobek, L. Chmatal, L. Mala, T. Ormsby, P. Angelisova, V. Horejsi, T. Brdicka
- 520 9_
- $a Transmembrane adaptor proteins are membrane-anchored proteins consisting of a short extracellular part, a transmembrane domain, and a cytoplasmic part with various protein-protein interaction motifs but lacking any enzymatic activity. They participate in the regulation of various signaling pathways by recruiting other proteins to the proximity of cellular membranes where the signaling is often initiated and propagated. In this work, we show that LST1/A, an incompletely characterized protein encoded by MHCIII locus, is a palmitoylated transmembrane adaptor protein. It is expressed specifically in leukocytes of the myeloid lineage, where it localizes to the tetraspanin-enriched microdomains. In addition, it binds SHP-1 and SHP-2 phosphatases in a phosphotyrosine-dependent manner, facilitating their recruitment to the plasma membrane. These data suggest a role for LST1/A in negative regulation of signal propagation.
- 650 _2
- $a sekvence aminokyselin $7 D000595
- 650 _2
- $a buněčná membrána $x metabolismus $7 D002462
- 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 _2
- $a hlavní histokompatibilní komplex $x fyziologie $7 D008285
- 650 _2
- $a membránové proteiny $x chemie $x genetika $x metabolismus $7 D008565
- 650 _2
- $a molekulární sekvence - údaje $7 D008969
- 650 _2
- $a myeloidní buňky $x cytologie $x metabolismus $7 D022423
- 650 _2
- $a plakiny $x metabolismus $7 D051179
- 650 _2
- $a primární buněčná kultura $7 D061251
- 650 _2
- $a terciární struktura proteinů $x fyziologie $7 D017434
- 650 _2
- $a transport proteinů $x fyziologie $7 D021381
- 650 _2
- $a tyrosinfosfatasa nereceptorového typu 11 $x metabolismus $7 D054592
- 650 _2
- $a tyrosinfosfatasa nereceptorového typu 6 $x metabolismus $7 D053824
- 650 _2
- $a pseudopodia $x metabolismus $7 D011554
- 650 _2
- $a signální transdukce $x fyziologie $7 D015398
- 650 _2
- $a U937 buňky $7 D020298
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Štěpánek, Ondřej $7 xx0246557 $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic
- 700 1_
- $a Hrdinka, M. $7 xx0271797 $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic
- 700 1_
- $a Drobek, Aleš $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic $7 xx0210358
- 700 1_
- $a Chmatal, Lukas $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic
- 700 1_
- $a Mala, Linda $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic
- 700 1_
- $a Ormsby, Tereza $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic
- 700 1_
- $a Angelisová, Pavla $7 xx0072996 $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic
- 700 1_
- $a Hořejší, Václav, $d 1949- $7 jn20000401057 $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic
- 700 1_
- $a Brdička, Tomáš $7 xx0140497 $u Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic
- 773 0_
- $w MED00002546 $t The Journal of biological chemistry $x 1083-351X $g Roč. 287, č. 27 (2012), s. 22812-22821
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/22589543 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20121023 $b ABA008
- 991 __
- $a 20170131075327 $b ABA008
- 999 __
- $a ok $b bmc $g 956513 $s 792000
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2012 $b 287 $c 27 $d 22812-22821 $i 1083-351X $m The Journal of biological chemistry $n J Biol Chem $x MED00002546
- LZP __
- $b NLK112 $a Pubmed-20121023
