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PMID:16139227

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Citation

Enomoto, A, Murakami, H, Asai, N, Morone, N, Watanabe, T, Kawai, K, Murakumo, Y, Usukura, J, Kaibuchi, K and Takahashi, M (2005) Akt/PKB regulates actin organization and cell motility via Girdin/APE. Dev. Cell 9:389-402

Abstract

The serine/threonine kinase Akt (also called protein kinase B) is well known as an important regulator of cell survival and growth and has also been shown to be required for cell migration in different organisms. However, the mechanism by which Akt functions to promote cell migration is not understood. Here, we identify an Akt substrate, designated Girdin/APE (Akt-phosphorylation enhancer), which is an actin binding protein. Girdin expresses ubiquitously and plays a crucial role in the formation of stress fibers and lamellipodia. Akt phosphorylates serine at position 1416 in Girdin, and phosphorylated Girdin accumulates at the leading edge of migrating cells. Cells expressing mutant Girdin, in which serine 1416 was replaced with alanine, formed abnormal elongated shapes and exhibited limited migration and lamellipodia formation. These findings suggest that Girdin is essential for the integrity of the actin cytoskeleton and cell migration and provide a direct link between Akt and cell motility.

Links

PubMed Online version:10.1016/j.devcel.2005.08.001

Keywords

Actins/metabolism; Animals; COS Cells; Cell Membrane/metabolism; Cell Movement/physiology; Cercopithecus aethiops; Humans; Microfilament Proteins; Microscopy, Electron; Phosphorylation; Protein-Serine-Threonine Kinases/metabolism; Proto-Oncogene Proteins/metabolism; Proto-Oncogene Proteins c-akt; RNA, Small Interfering/genetics; RNA, Small Interfering/metabolism; Vero Cells; Vesicular Transport Proteins/genetics; Vesicular Transport Proteins/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:AKT1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q3V6T2

F

Seeded From UniProt

complete

HUMAN:GRDN

located_in

GO:0030027: lamellipodium

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:AKT1

enables

GO:0004674: protein serine/threonine kinase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:AKT1

involved_in

GO:0018105: peptidyl-serine phosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:GRDN

involved_in

GO:0030032: lamellipodium assembly

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:GRDN

part_of

GO:0030027: lamellipodium

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:GRDN

enables

GO:0043422: protein kinase B binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P31749

F

Seeded From UniProt

complete

HUMAN:GRDN

enables

GO:0042803: protein homodimerization activity

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q3V6T2

F

Seeded From UniProt

complete

HUMAN:GRDN

enables

GO:0035091: phosphatidylinositol binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:GRDN

involved_in

GO:0032956: regulation of actin cytoskeleton organization

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:GRDN

involved_in

GO:0016477: cell migration

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:GRDN

enables

GO:0003779: actin binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:GRDN

GO:0051496: positive regulation of stress fiber assembly

ECO:0000315:

P

Figure 4B and 5C

complete
CACAO 10957


See also

References

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