Abstract
Upon binding to their ligand, several growth factor receptors that contain a tyrosine kinase within their cytoplasmic domain [receptor tyrosine kinases (RTKs)] induce a substantial reorganization of the actin cytoskeleton. This change in actin superstructure is necessary to produce multiple motile responses within the target cells. RTKs catalyse the clustering of effector proteins within functional units underneath the plasma membrane. Upon reaching a critical mass, RTK-effector units send out signals through the metabolism of membrane phospholipids and other second messenger molecules that regulate the interaction of actin with its satellite regulatory molecules. Several actin binding proteins interact transiently with small clusters of membrane inositol phospholipids in vitro (4 to 5 phospholipid molecules per actin binding protein). Such transient complex formation can either down-regulate or up-regulate the interaction of regulatory proteins with actin. The phospholipids involved in the surface catalytic control of the actin cytoskeleton are metabolically very active and abundant in cells, and are therefore poised to mediate reactions linking signal transduction molecules to the reorganization of the actin cytoskeleton upon cell activation.
| Original language | English |
|---|---|
| Pages (from-to) | 201-208 |
| Number of pages | 8 |
| Journal | Seminars in Cell and Developmental Biology |
| Volume | 5 |
| Issue number | 3 |
| State | Published - Dec 1 1994 |
| Externally published | Yes |
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Keywords
- Actin
- Actin binding proteins
- Cell signaling
- Phospholipase
- Receptor tyrosine kinase
ASJC Scopus subject areas
- Developmental Biology
- Medicine(all)
Cite this
Growth factor receptors, phospholipases, phospholipid kinases and actin reorganization. / Gips, Sanford J.; Kandzari, David E.; Goldschmidt-Clermont, Pascal.
In: Seminars in Cell and Developmental Biology, Vol. 5, No. 3, 01.12.1994, p. 201-208.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Growth factor receptors, phospholipases, phospholipid kinases and actin reorganization
AU - Gips, Sanford J.
AU - Kandzari, David E.
AU - Goldschmidt-Clermont, Pascal
PY - 1994/12/1
Y1 - 1994/12/1
N2 - Upon binding to their ligand, several growth factor receptors that contain a tyrosine kinase within their cytoplasmic domain [receptor tyrosine kinases (RTKs)] induce a substantial reorganization of the actin cytoskeleton. This change in actin superstructure is necessary to produce multiple motile responses within the target cells. RTKs catalyse the clustering of effector proteins within functional units underneath the plasma membrane. Upon reaching a critical mass, RTK-effector units send out signals through the metabolism of membrane phospholipids and other second messenger molecules that regulate the interaction of actin with its satellite regulatory molecules. Several actin binding proteins interact transiently with small clusters of membrane inositol phospholipids in vitro (4 to 5 phospholipid molecules per actin binding protein). Such transient complex formation can either down-regulate or up-regulate the interaction of regulatory proteins with actin. The phospholipids involved in the surface catalytic control of the actin cytoskeleton are metabolically very active and abundant in cells, and are therefore poised to mediate reactions linking signal transduction molecules to the reorganization of the actin cytoskeleton upon cell activation.
AB - Upon binding to their ligand, several growth factor receptors that contain a tyrosine kinase within their cytoplasmic domain [receptor tyrosine kinases (RTKs)] induce a substantial reorganization of the actin cytoskeleton. This change in actin superstructure is necessary to produce multiple motile responses within the target cells. RTKs catalyse the clustering of effector proteins within functional units underneath the plasma membrane. Upon reaching a critical mass, RTK-effector units send out signals through the metabolism of membrane phospholipids and other second messenger molecules that regulate the interaction of actin with its satellite regulatory molecules. Several actin binding proteins interact transiently with small clusters of membrane inositol phospholipids in vitro (4 to 5 phospholipid molecules per actin binding protein). Such transient complex formation can either down-regulate or up-regulate the interaction of regulatory proteins with actin. The phospholipids involved in the surface catalytic control of the actin cytoskeleton are metabolically very active and abundant in cells, and are therefore poised to mediate reactions linking signal transduction molecules to the reorganization of the actin cytoskeleton upon cell activation.
KW - Actin
KW - Actin binding proteins
KW - Cell signaling
KW - Phospholipase
KW - Receptor tyrosine kinase
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M3 - Article
C2 - 7919234
AN - SCOPUS:0028451037
VL - 5
SP - 201
EP - 208
JO - Seminars in Cell and Developmental Biology
JF - Seminars in Cell and Developmental Biology
SN - 1084-9521
IS - 3
ER -