|
Envelope surface glycoprotein gp120
|
env
|
The ability of gp120 to inhibit SDF-1alpha-induced chemotaxis is mediated by the CD4 receptor and Lck signaling |
PubMed
|
|
env
|
Interaction of HIV-1 gp120 with CD4 leads to increased levels of phosphorylation of the src-family Lck and Fyn protein tyrosine kinases and enhancement of their activities |
PubMed
|
|
env
|
HIV-1 gp120 induces the dissociation of p56lck from CD4 and the downregulation of CD4 from the cellular surface |
PubMed
|
|
env
|
Binding of HIV-1 gp120 to CD4 induces p56lck activation and zeta-chain (TCR) associated protein kinase 70kDa desensitization independent of TCR tyrosine phosphorylation |
PubMed
|
|
env
|
Engagement of CD4 with HIV-1 gp120 inhibits Lck and F-actin recruitment into the immunological synapse |
PubMed
|
|
env
|
The protein tyrosine kinase p56lck plays an active role in transmitting an HIV-1 gp120-mediated signal that increases the oxidative state of cells and as a consequence amplifies TNF-mediated NF-kappa B DNA binding |
PubMed
|
|
env
|
HIV-1 gp120 induces an increase in tyrosine phosphorylation of two proteins, p56lck and phosphatidylinositol 3-kinase (PI 3-kinase) p85 alpha, that are physically complexed to the CD4 molecule |
PubMed
|
|
env
|
HIV-1 gp120 inhibits CD3-induced Lck activation and cellular tyrosine phosphorylation, particularly of phosphoinositide-specific phospholipase C-gamma-1 |
PubMed
|
|
env
|
CD4-p56Lck interaction is required for HIV-1 gp120-induced nuclear translocation of NF-kappaB in HeLa cells |
PubMed
|
|
env
|
p56lck-positive cells are markedly more susceptible to syncytium formation than p56lck-negative cells, implying a regulatory role for p56lck in the syncytium formation mediated by HIV-1 gp120 envelope interaction with CD4 |
PubMed
|
|
env
|
Binding of HIV-1 gp120 to CD4 molecules results in the association of Lck and Raf-1, which is abolished by preincubation of the virus with soluble CD4 |
PubMed
|
|
env
|
Activation of the CD4-p56lck receptor signal transduction pathway by HIV-1 gp120 does not increase prostaglandin formation |
PubMed
|
|
Envelope surface glycoprotein gp160, precursor
|
env
|
Interaction of HIV-1 gp160 with CD4 increases p56lck autophosphorylation and kinase activity |
PubMed
|
|
env
|
HIV-1 gp160 downregulates lymphocyte function-associated antigen-1 (LFA-1)-dependent adhesion between CD4+ T cells and B cells; this downregulation is shown to be p56lck-dependent |
PubMed
|
|
Envelope transmembrane glycoprotein gp41
|
env
|
HIV-1 gp120 and gp41-induced cell killing is accompanied by tyrosine phosphorylation and activation of the CD4-associated p56(Lck) kinase, and by activation of a second member of the scr family of protein tyrosine kinases, p59(fyn) kinase |
PubMed
|
|
Nef
|
nef
|
HIV-1 NL4-3 Nef recruits LCK (p56) into endosomes, which is dependent upon the CPG-motif of Nef |
PubMed
|
|
nef
|
HIV-1 Nef-induced relocalization of LCK is correlated with N-Ras activation at recycling endosome/TGN compartments |
PubMed
|
|
nef
|
HIV-1 Nef induces relocalization of LCK away from the plasma membrane to the recycling endosome and the trans-Golgi network, inhibiting recruitment of LCK to the immunological synapse |
PubMed
|
|
nef
|
HIV-1 Nef increases the association of the src family tyrosine kinase, Lck, and TCRzeta with rafts in human T cells, suggesting Nef primes resting T cells for activation by upregulating the levels of signaling molecules within rafts |
PubMed
|
|
nef
|
HIV-1 Nef efficiently interacts with Lck by coimmunoprecipitation and in vitro kinase assays; this interaction is reduced by an R71T mutation in the proline-rich motif of Nef |
PubMed
|
|
nef
|
The formation of Nef/LCK/PKCtheta complex activates the ERK MAPK signaling pathway |
PubMed
|
|
nef
|
HIV-1 Nef interferes with the activation of Lck and as a consequence of signaling via the IL-2 receptor |
PubMed
|
|
nef
|
Cooperation of the Lck SH2 and SH3 domains is required for HIV-1 Nef binding to Lck to a level similar to Nef binding to the Hck SH3 domain |
PubMed
|
|
nef
|
The HIV-1 Nef highly conserved valine-glycine-phenylalanine amino acid triplet (VGF) motif is essential for effects of Nef on actin dynamics and Lck localization |
PubMed
|
|
nef
|
Expression of SH3/SH2 ligand-uncoordinated 119 (UNC119) completely reverses the HIV-1 Nef-mediated inhibition of immunological synapse recruitment of LCK |
PubMed
|
|
nef
|
HIV-1 Nef-induced relocalization of LCK increases phosphorylated ERK1/2 induction in infected and trasduced primary T cells |
PubMed
|
|
nef
|
HIV-1 Nef induces intracellular accumulation of Lck and interferes with its recruitment to sites of TCR engagement. The accumulation of Lck requires the membrane attachment G2 and the SH3 binding motif AXXA of Nef |
PubMed
|
|
nef
|
Human T cells expressing herpes virus saimiri-Tip mediate restriction of late-stage replication of HIV-1 by disrupting Nef interaction with Lck in lipid rafts |
PubMed
|
|
nef
|
Formation of the Nef-associated kinase complex (NAKC) is sufficient to activate LCK and ERK1/2 and causes a strong Tat-dependent increase of HIV-1 transcription in T cells |
PubMed
|
|
nef
|
In the context of Nef-associated kinase complex (NAKC), hnRNP-K interacts with HIV-1 Nef and recruits LCK, PKCdelta, and PI-3 kinase. The proline-rich domain (amino-acids 289-315) of hnRNP-K is required for the recruitment of activated LCK18854243 |
PubMed
|
|
nef
|
PKCtheta is a downstream effector of LCK and is recruited by HIV-1 Nef to form the Nef/LCK/PKCtheta complex, which promotes HIV transcription |
PubMed
|
|
nef
|
HIV-1 Nef-mediated increase of HIV transcription requires the Nef N terminus (amino acids 12-29) and LCK kinase activity by Nef activation |
PubMed
|
|
nef
|
Expression of p56(lck) in nonlymphoid CD4-expressing cells restores the ability of Nef in order to increase the internalization rate of CD4 |
PubMed
|
|
nef
|
HIV-1 Nef increases the production of exosomes, which form at the plasma membrane and co-localizes with plasma membrane-associated proteins ICAM1, CD81, and Lck in Jurkat |
PubMed
|
|
nef
|
Amino acid residues 402-419 of the cytoplasmic tail of CD4 are required for association with Lck and also for the downregulation of CD4 induced by HIV-1 Nef, suggesting a potential interaction between Nef and Lck |
PubMed
|
|
nef
|
HIV-1 and SIV Nef can bind Lck SH2 domains, and their N-terminal 50 amino acid residues are sufficient for Src kinase binding and activation |
PubMed
|
|
nef
|
Assays with phage-displayed Nef from HIV-1 NL4-3 have been used to identify a series of guanidine alkaloid-based inhibitors of Nef interactions with p53, actin, and p56(lck) |
PubMed
|
|
nef
|
A highly conserved proline-rich repeat sequence in Nef between amino acids 69-78 directly binds to the SH2 and SH3 domains of Lck |
PubMed
|
|
nef
|
HIV-1 Nef enhances the phosphorylation of c-Cbl in CD4+ T cells, an effect that requires the Src tyrosine kinase Lck |
PubMed
|
|
Pr55(Gag)
|
gag
|
The amplified luminescent proximity homogeneous assay (AlphaScreen) identifies the interaction of HIV-1 Gag with LCK |
PubMed
|
|
gag
|
Lck enhances HIV-1 Gag assembly and release in T cells. Lck palmitoylation sites at cysteine's 3 and 5 are required for the efficient virus production |
PubMed
|
|
Tat
|
tat
|
Herpes virus saimiri-StpC synergizes with Tat during transcriptional activation of the HIV-1 LTR. This transcriptional synergy between StpC and Tat requires Lck and NF-kappaB consensus binding sequences |
PubMed
|
|
tat
|
Formation of the Nef-associated kinase complex (NAKC) is sufficient to activate LCK and ERK1/2 and causes a strong Tat-dependent increase of HIV-1 transcription in T cells |
PubMed
|
|
tat
|
HIV-1 Tat activates p56lck in Jurkat cells leading to the degradation of IkappaBalpha and activation of NFkappaB, AP-1, JNK, MAPKK, caspases, and apoptosis |
PubMed
|
|
Vpu
|
vpu
|
HIV-1 Vpu affects the subcellular localization of LCK but with reduced efficacy compared to HIV-1 Nef |
PubMed
|