U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    HCLS1 hematopoietic cell-specific Lyn substrate 1 [ Homo sapiens (human) ]

    Gene ID: 3059, updated on 3-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Correlation between elevated HCLS1 levels and heart failure: A diagnostic biomarker.

    Correlation between elevated HCLS1 levels and heart failure: A diagnostic biomarker.
    Li C, Zhang L, Zhang L, Zhang G., Free PMC Article

    10/30/2024
    Hematopoietic cell-specific Lyn substrate, HCLS1, is a versatile actin-binding protein in leukocytes. (Review)

    Hematopoietic cell-specific lyn substrate (HCLS1 or HS1): A versatile actin-binding protein in leukocytes.
    Castro-Ochoa KF, Guerrero-Fonseca IM, Schnoor M.

    05/9/2020
    these studies indicate HS1 plays an important role in ROR1-dependent Wnt5a-enhanced chemokine-directed leukemia-cell migration.

    Wnt5a induces ROR1 to complex with HS1 to enhance migration of chronic lymphocytic leukemia cells.
    Hasan MK, Yu J, Chen L, Cui B, Widhopf Ii GF, Rassenti L, Shen Z, Briggs SP, Kipps TJ., Free PMC Article

    12/16/2017
    SDF1alpha-induced interaction of the adapter proteins Nck and HS1 facilitates actin polymerization and migration in T cells.

    SDF1α-induced interaction of the adapter proteins Nck and HS1 facilitates actin polymerization and migration in T cells.
    Lettau M, Kabelitz D, Janssen O.

    04/18/2015
    Phosphoproteome analyses reveal specific implications of Hcls1, p21-activated kinase 1 and Ezrin in proliferation of a myeloid progenitor cell line downstream of wild-type and ITD mutant Fms-like tyrosine kinase 3 receptors.

    Phosphoproteome analyses reveal specific implications of Hcls1, p21-activated kinase 1 and Ezrin in proliferation of a myeloid progenitor cell line downstream of wild-type and ITD mutant Fms-like tyrosine kinase 3 receptors.
    Habif G, Grasset MF, Kieffer-Jaquinod S, Kuhn L, Mouchiroud G, Gobert-Gosse S.

    07/6/2013
    interaction of HCLS1 with LEF-1 is essential for G-CSF-triggered myeloid differentiation; data demonstrate the importance of HCLS1 in myelopoiesis in vitro and in vivo

    Interactions among HCLS1, HAX1 and LEF-1 proteins are essential for G-CSF-triggered granulopoiesis.
    Skokowa J, Klimiankou M, Klimenkova O, Lan D, Gupta K, Hussein K, Carrizosa E, Kusnetsova I, Li Z, Sustmann C, Ganser A, Zeidler C, Kreipe HH, Burkhardt J, Grosschedl R, Welte K., Free PMC Article

    01/12/2013
    HS1 overexpressed in leukemic as compared to normal B lymphocytes.

    HS1, a Lyn kinase substrate, is abnormally expressed in B-chronic lymphocytic leukemia and correlates with response to fludarabine-based regimen.
    Frezzato F, Gattazzo C, Martini V, Trimarco V, Teramo A, Carraro S, Cabrelle A, Ave E, Facco M, Zambello R, Tibaldi E, Brunati AM, Semenzato G, Trentin L., Free PMC Article

    12/8/2012
    a novel role for HS1 and its phosphorylation during neutrophil directed migration.

    The actin regulatory protein HS1 interacts with Arp2/3 and mediates efficient neutrophil chemotaxis.
    Cavnar PJ, Mogen K, Berthier E, Beebe DJ, Huttenlocher A., Free PMC Article

    10/20/2012
    High HS1 expression predicts poor survival of chronic lymphocytic leukemia patients.

    High expression of hematopoietic cell specific Lyn substrate-1 (HS1) predicts poor survival of B-cell chronic lymphocytic leukemia patients.
    Butrym A, Majewski M, Dzietczenia J, Kuliczkowski K, Mazur G.

    08/4/2012
    SH3 domain of HS1 protein recognizes lysine-rich polyproline motifs.

    The SH3 domain of HS1 protein recognizes lysine-rich polyproline motifs.
    Siligardi G, Ruzza P, Hussain R, Cesaro L, Brunati AM, Pinna LA, Donella-Deana A.

    06/30/2012
    HS1 is a central regulator of cytoskeleton remodeling that controls lymphocyte trafficking and homing and significantly influences the tissue invasion and infiltration in chronic lymphocytic leukemia.

    HS1 has a central role in the trafficking and homing of leukemic B cells.
    Scielzo C, Bertilaccio MT, Simonetti G, Dagklis A, ten Hacken E, Fazi C, Muzio M, Caiolfa V, Kitamura D, Restuccia U, Bachi A, Rocchi M, Ponzoni M, Ghia P, Caligaris-Cappio F.

    01/1/2011
    Observational study of gene-disease association. (HuGE Navigator)

    Association of a four-amino acid residue insertion polymorphism of the HS1 gene with systemic lupus erythematosus: molecular and functional analysis.
    Otsuka J, Horiuchi T, Yoshizawa S, Tsukamoto H, Sawabe T, Kikuchi Y, Himeji D, Koyama T, Mitoma H, Watanabe T, Harada M.

    03/13/2008
    HS1 may play a role in cytoskeleon organization in B-cells and leukemic B-cells

    HS1 complexes with cytoskeleton adapters in normal and malignant chronic lymphocytic leukemia B cells.
    Muzio M, Scielzo C, Frenquelli M, Bachi A, De Palma M, Alessio M, Ghia P, Caligaris-Cappio F.

    01/21/2010
    found in cell types other than hematopoietic cells

    Expression of the gene for hematopoietic cell specific protein is not restricted to cells of hematopoietic origin.
    Fischer U, Michel A, Meese EU.

    01/21/2010
    TBB induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells.

    Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells.
    Ruzzene M, Penzo D, Pinna LA., Free PMC Article

    01/21/2010
    The HS1 coiled-coil region acts synergistically with the repeat domain in the modulation of the Arp2/3 complex-mediated actin polymerization.

    The coiled-coil domain is required for HS1 to bind to F-actin and activate Arp2/3 complex.
    Hao JJ, Zhu J, Zhou K, Smith N, Zhan X.

    01/21/2010
    substrate for caspase cleavage during apoptosis

    Caspase-mediated cleavage of actin-binding and SH3-domain-containing proteins cortactin, HS1, and HIP-55 during apoptosis.
    Chen YR, Kori R, John B, Tan TH.

    01/21/2010
    HS1 Tyr phosphorylation catalyzed by Syk and Lyn plays a crucial role in the translocation of the protein to the membrane and is involved in the cytoskeleton rearrangement triggered by thrombin in human platelets

    Thrombin-induced tyrosine phosphorylation of HS1 in human platelets is sequentially catalyzed by Syk and Lyn tyrosine kinases and associated with the cellular migration of the protein.
    Brunati AM, Deana R, Folda A, Massimino ML, Marin O, Ledro S, Pinna LA, Donella-Deana A.

    01/21/2010
    firstprevious page of 1 nextlast