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Hematopoietic cell‐specific lyn substrate (HCLS1 or HS1): A versatile actin‐binding protein in leukocytes
Author(s) -
CastroOchoa Karla F.,
GuerreroFonseca Idaira M.,
Schnoor Michael
Publication year - 2019
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.mr0618-212r
Subject(s) - biology , microbiology and biotechnology , lyn , cortactin , podosome , actin , actin remodeling , actin cytoskeleton , cytoskeleton , signal transduction , proto oncogene tyrosine protein kinase src , cell , genetics
Leukocytes are constantly produced in the bone marrow and released into the circulation. Many different leukocyte subpopulations exist that exert distinct functions. Leukocytes are recruited to sites of inflammation and combat the cause of inflammation via many different effector functions. Virtually all of these processes depend on dynamic actin remodeling allowing leukocytes to adhere, migrate, phagocytose, and release granules. However, actin dynamics are not possible without actin‐binding proteins (ABP) that orchestrate the balance between actin polymerization, branching, and depolymerization. The homologue of the ubiquitous ABP cortactin in hematopoietic cells is hematopoietic cell‐specific lyn substrate‐1, often called hematopoietic cell‐specific protein‐1 (HCLS1 or HS1). HS1 has been reported in different leukocytes to regulate Arp2/3‐dependent migration. However, more evidence is emerging that HS1 functions go far beyond just being a direct actin modulator. For example, HS1 is important for the activation of GTPases and integrins, and mediates signaling downstream of many receptors including BCR, TCR, and CXCR4. In this review, we summarize current knowledge on HS1 functions and discuss them in a pathophysiologic context.

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