FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2590708794> ?p ?o ?g. }

• W2590708794 abstract "Several members of the Src family of non-receptor protein tyrosine kinases (e.g. Yes), as well as Leishmania hydrophilic acylated surface protein B (HASPB) harbor a short N-terminal motif called the Src homology 4 (SH4) domain, which undergoes tandem modification with the saturated acyl chains myristate and palmitate. SH4 domains are responsible for stable anchoring of these otherwise soluble proteins to the cytoplasmic leaflet of cellular membranes, mediate their targeting to the plasma membrane, and moreover, confer affinity for cholesterol- and sphingolipid-enriched membrane microdomains, that is lipid rafts. N-terminal myristoylation occurs in the cytosol, concurrently with translation of the protein, and is a prerequisite for subsequent palmitoylation. The latter is thought to occur at perinuclear (most probably Golgi) membranes. It has been hypothesized that doubly acylated SH4 domain proteins partition into lipid rafts soon after being palmitoylated at the Golgi, and that these microdomains are necessary for the transport of SH4 proteins to the plasma membrane, by playing a role in their sorting and/or formation of transport carriers at the trans-Golgi network.The aim of the first part of this study was to characterize membrane (both lipid and protein) environment of diacylated SH4 domain proteins residing in lipid rafts. The approach was to analyze lipid and protein components of immunoaffinity-purified detergent-resistant membranes (DRMs) containing SH4 domain reporter fusion proteins. DRMs immunoisolated using a HASPB SH4 domain fusion protein as bait differed in lipid composition from the total DRM pool, being enriched in sphingomyelin, and depleted in phosphatidylcholine and phosphatidylethanolamine, and therefore seem to be a subset of total DRMs. This may suggest that in vivo, the protein associates with a specific subset of lipid rafts, thus indicating that the heterogeneity of lipid rafts can be appreciated also using the detergent method. Our immunoaffinity purification approach seemed to enrich for bona fide raft proteins, as suggested by an increase compared to total DRMs in the proportion of plasma membrane and lipid-anchored proteins, as well as proteins whose association with DRMs is sensitive to cholesterol depletion. We estimated relative amounts of proteins in immunoisolated SH4 DRMs and total DRMs, with the use of label-free mass spectrometry-based quantification, which was validated for a subset of proteins by quantitative Western blotting. We could observe a lack of enrichment of endogenous Yes kinase in immunoisolated SH4 DRMs, which may indicate that the identity of lipid rafts into which SH4 domain proteins partition, is determined not only by the dual fatty acylation with myristate and palmitate, but also by interactions conferred by domains distal from the SH4 domain.In the second part of this study, we intended to investigate the previously reported role of the COPI coatomer complex, as well as of the secretory pathway in general, in the plasma membrane transport of diacylated SH4 domain proteins. Conditions that disrupted the structure and function of the Golgi apparatus, i.e. siRNA-mediated knockdown of the β subunit of the COPI complex, expression of constitutively active mutant (Q71L) of the small GTPase Arf1, as well as brefeldin A treatment, resulted in increased intracellular accumulation of a HASPB SH4 fluorescent fusion protein, pointing out to the role of the Golgi in its transport to the plasma membrane. None of the above treatments, however, blocked the appearance of the SH4 reporter protein at the plasma membrane, suggesting the existence of an alternative trafficking pathway that does not require the Golgi complex." @default.
• W2590708794 created "2017-03-03" @default.
• W2590708794 creator A5025748801 @default.
• W2590708794 date "2013-01-01" @default.
• W2590708794 modified "2023-09-23" @default.
• W2590708794 title "Diacylated SH4 domain proteins: studies on their lipid and protein environment at the plasma membrane and intracellular transport" @default.
• W2590708794 cites W1475896266 @default.
• W2590708794 cites W1494227533 @default.
• W2590708794 cites W1535587662 @default.
• W2590708794 cites W1570306557 @default.
• W2590708794 cites W1576433430 @default.
• W2590708794 cites W1579191879 @default.
• W2590708794 cites W1580161657 @default.
• W2590708794 cites W1593795070 @default.
• W2590708794 cites W1601798272 @default.
• W2590708794 cites W1603362495 @default.
• W2590708794 cites W161143260 @default.
• W2590708794 cites W1633066991 @default.
• W2590708794 cites W1672154570 @default.
• W2590708794 cites W1841488655 @default.
• W2590708794 cites W1890859862 @default.
• W2590708794 cites W1939198418 @default.
• W2590708794 cites W1944304173 @default.
• W2590708794 cites W1964252660 @default.
• W2590708794 cites W1964480443 @default.
• W2590708794 cites W1964598018 @default.
• W2590708794 cites W1965260691 @default.
• W2590708794 cites W1965336618 @default.
• W2590708794 cites W1966998035 @default.
• W2590708794 cites W1967131697 @default.
• W2590708794 cites W1968774879 @default.
• W2590708794 cites W1969312560 @default.
• W2590708794 cites W1969461041 @default.
• W2590708794 cites W1970160164 @default.
• W2590708794 cites W1970196085 @default.
• W2590708794 cites W1970353708 @default.
• W2590708794 cites W1971837853 @default.
• W2590708794 cites W1972290108 @default.
• W2590708794 cites W1974282614 @default.
• W2590708794 cites W1974928798 @default.
• W2590708794 cites W1975791322 @default.
• W2590708794 cites W1978281474 @default.
• W2590708794 cites W1978424789 @default.
• W2590708794 cites W1978542424 @default.
• W2590708794 cites W1978661786 @default.
• W2590708794 cites W1978683809 @default.
• W2590708794 cites W1978686382 @default.
• W2590708794 cites W1978701884 @default.
• W2590708794 cites W1981593008 @default.
• W2590708794 cites W1983203888 @default.
• W2590708794 cites W1983657784 @default.
• W2590708794 cites W1984730682 @default.
• W2590708794 cites W1986827801 @default.
• W2590708794 cites W1987179671 @default.
• W2590708794 cites W1987971027 @default.
• W2590708794 cites W1990044954 @default.
• W2590708794 cites W1991402029 @default.
• W2590708794 cites W1991655565 @default.
• W2590708794 cites W1991683855 @default.
• W2590708794 cites W1995802547 @default.
• W2590708794 cites W1996988785 @default.
• W2590708794 cites W1997957872 @default.
• W2590708794 cites W1998697778 @default.
• W2590708794 cites W1998865212 @default.
• W2590708794 cites W1998917031 @default.
• W2590708794 cites W1999417865 @default.
• W2590708794 cites W2000456126 @default.
• W2590708794 cites W2000638372 @default.
• W2590708794 cites W2001819758 @default.
• W2590708794 cites W2001977025 @default.
• W2590708794 cites W2003178039 @default.
• W2590708794 cites W2003625629 @default.
• W2590708794 cites W2004763373 @default.
• W2590708794 cites W2007674710 @default.
• W2590708794 cites W2008009726 @default.
• W2590708794 cites W2008817350 @default.
• W2590708794 cites W2011800776 @default.
• W2590708794 cites W2014030143 @default.
• W2590708794 cites W2014503023 @default.
• W2590708794 cites W2015556811 @default.
• W2590708794 cites W2015763826 @default.
• W2590708794 cites W2015800932 @default.
• W2590708794 cites W2016055694 @default.
• W2590708794 cites W2017264694 @default.
• W2590708794 cites W2018400595 @default.
• W2590708794 cites W2020279663 @default.
• W2590708794 cites W2022653182 @default.
• W2590708794 cites W2027327211 @default.
• W2590708794 cites W2028858498 @default.
• W2590708794 cites W2030202169 @default.
• W2590708794 cites W2030214706 @default.
• W2590708794 cites W2030602313 @default.
• W2590708794 cites W2030939970 @default.
• W2590708794 cites W2032062053 @default.
• W2590708794 cites W2034512365 @default.
• W2590708794 cites W2035562653 @default.
• W2590708794 cites W2035807916 @default.
• W2590708794 cites W2036321220 @default.
• W2590708794 cites W2036420384 @default.
• W2590708794 cites W2037582316 @default.

• next