The src protein contains multiple domains for specific attachment to membranes.
about
Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolaeAmino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipidsIdentification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipidsAnnexin 2 has a dual role as regulator and effector of v-Src in cell transformationLipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism.The C terminus of c-Src inhibits breast tumor cell growth by a kinase-independent mechanism.Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling.Polyomavirus middle-T antigen associates with the kinase domain of Src-related tyrosine kinases.Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527.Csk suppression of Src involves movement of Csk to sites of Src activity.Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.Tyrosine phosphorylation of three cellular proteins correlates with transformation of rat 1 cells by pp60src.Expression of p60v-src in Saccharomyces cerevisiae results in elevation of p34CDC28 kinase activity and release of the dependence of DNA replication on mitosisSelected glimpses into the activation and function of Src kinase.Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: theory and experimentCharacterization of mice deficient in the Src family nonreceptor tyrosine kinase Frk/rakPhosphorylation controls a dual-function polybasic nuclear localization sequence in the adapter protein SH2B1β to regulate its cellular function and distributionA novel nuclear Src and p300 signaling axis controls migratory and invasive behavior in pancreatic cancer.Gag influences transformation by Abelson murine leukemia virus and suppresses nuclear localization of the v-Abl proteinImmunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells.The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity.Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations.Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae.Mutagenesis of the 43-kD postsynaptic protein defines domains involved in plasma membrane targeting and AChR clusteringSpecific association of the proto-oncogene product pp60c-src with an intracellular organelle, the PC12 synaptic vesicleLysine residues form an integral component of a novel NH2-terminal membrane targeting motif for myristylated pp60v-src.Association of p60c-src with endosomal membranes in mammalian fibroblastsMyristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis.The ADP/ATP carrier is the 32-kilodalton receptor for an NH2-terminally myristylated src peptide but not for pp60src polypeptideA myristylated form of the sea oncoprotein can transform chicken embryo fibroblastsSuppression of retroviral MA deletions by the amino-terminal membrane-binding domain of p60src.The amino-terminal 14 amino acids of v-src can functionally replace the extracellular and transmembrane domains of v-erbB.Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways.Exploring proteome-wide occurrence of clusters of charged residues in eukaryotes.Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release.Two point mutations in the transmembrane domain of P68gag-ros inactive its transforming activity and cause a delay in membrane association.Myristylation is involved in intracellular retention of hepatitis B virus envelope proteins.Effect of a membrane-targeted sphingosine kinase 1 on cell proliferation and survival.Does the binding of clusters of basic residues to acidic lipids induce domain formation in membranes?Nonmyristoylated Abl proteins transform a factor-dependent hematopoietic cell line.
P2860
Q24323219-207A2ED5-9B56-446D-8D36-7ADACB084DCBQ24564497-33F6E9C3-A25D-4BD3-BE36-B52B62C78255Q24646680-B5D28928-BDF8-484A-A663-5A05B230B601Q28570986-8C95CFD0-06B7-41FB-B300-E6A641DD9EA7Q30009924-4EAF3A43-BD24-48A8-96AC-71509E4C0FA4Q30164215-423B3B6E-55DE-4349-A90D-08C8578DD410Q30176895-D8C23C53-504E-4D77-992C-0E2C970039DAQ30177032-0AD396E1-8749-4D92-A5F0-B1D93D3655B6Q30194001-0EBED139-A937-461F-A18B-6FB5DAC05A75Q30194179-E016B894-B2F0-4D49-A75F-ED2E9D1A82D2Q30194837-F167FEA5-93C1-48B3-9FBD-7A38E2231D99Q30442121-CC51FF1A-33B6-4D3B-9FF5-F8563DC70907Q30450260-F5E08E65-840E-4842-9EF5-06E518EA03EBQ34103644-550E0B13-FA02-4912-94BC-E4075868C3F8Q34171993-3D208128-3136-4644-B89F-CBAD3750990EQ34441584-77681FFC-323A-4774-9109-3906EAD61F1EQ34808684-58482E03-28C2-4681-A9B7-FC865F2A3A5AQ35875878-B7286C01-4423-47AD-AF6C-EE53348A6D58Q35947927-C10E2475-1973-4259-B393-D4A2BE93371FQ36224251-47C68E32-637A-485B-9580-34AF91300EC1Q36233735-3925A083-5D21-4AA5-8CC3-2FCC89E42E80Q36277661-4C053994-543F-41D4-9A9D-9644D53A2AA1Q36382857-11356F6A-1112-4262-B1ED-13ADABEF2FEEQ36530547-E4FCEB86-7EA2-4E64-A471-C9E776C78A5CQ36531435-A5BFD450-3649-4CF5-98CE-40A125C7CAD1Q36532023-D601F757-D2A5-4260-8771-DD16D1C769D0Q36533201-E01CABFC-6A86-491A-BCAB-4202F890A64AQ36675443-5E0D67D1-70F4-4252-AF06-CAB71E5D7E36Q36683013-F1A9C2C7-A3EC-4874-9F6A-8DCBCF4EA947Q36688971-69582217-5044-4D13-85C1-3D3678F7C351Q36701556-9E06BCD1-FD9B-4DDB-8FDF-86A1F5023B47Q36732985-BEACDFE0-F7DE-4473-BAFE-6922AE582922Q38354870-7EAC4C24-2C0C-43BC-B0A8-4EB245973152Q38463331-96B06957-F484-49FE-B798-8D6D65022F58Q40047075-693AC159-A2E2-4F24-8730-EBB775085FDCQ40062544-4958AE1E-27E8-4EC0-8D8D-04919D69486DQ40067346-10E1C6A6-2E30-4C7F-AB04-E0DDF709C9F6Q40461757-6A5DC78B-0AD5-4C24-A727-A5A59A9CFE7DQ40536955-104C35AE-B839-4B50-90BA-BFBC64B45EA1Q40678630-CA8A35DA-2057-4152-A951-51E46BABB87B
P2860
The src protein contains multiple domains for specific attachment to membranes.
description
1990 nî lūn-bûn
@nan
1990 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի մարտին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
The src protein contains multiple domains for specific attachment to membranes.
@ast
The src protein contains multiple domains for specific attachment to membranes.
@en
The src protein contains multiple domains for specific attachment to membranes.
@nl
type
label
The src protein contains multiple domains for specific attachment to membranes.
@ast
The src protein contains multiple domains for specific attachment to membranes.
@en
The src protein contains multiple domains for specific attachment to membranes.
@nl
prefLabel
The src protein contains multiple domains for specific attachment to membranes.
@ast
The src protein contains multiple domains for specific attachment to membranes.
@en
The src protein contains multiple domains for specific attachment to membranes.
@nl
P2860
P356
P1476
The src protein contains multiple domains for specific attachment to membranes.
@en
P2093
J M Kaplan
P2860
P304
P356
10.1128/MCB.10.3.1000
P407
P577
1990-03-01T00:00:00Z