The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton

Randazzo, Paul A.; Andrade, Josefa; Miura, Koichi; Brown, Megan T.; Long, Ya‐Qiu; Stauffer, Stacey; Roller, Peter P.; Cooper, Jonathan A.

doi:10.1073/pnas.070552297

Cited by 203 publications

(206 citation statements)

References 63 publications

Supporting

Mentioning

182

Contrasting

Unclassified

Order By: Relevance

“…(Someya et al, 2001) and promotes GDP/GTP exchange on ARF6. The small GTPase ARF6 is a plasma membrane-localized protein and functions in the regulation of membrane ruffling, cell motility, aspects of endocytosis and exocytosis, membrane recycling, reorganization of the cortical actin cytoskeleton and activation of phospholipase D (Kondo et al, 2000;Radhakrishna et al, 1999;Randazzo et al, 2000;Turner and Brown, 2001). In Drosophila Arf6 is remarkably well conserved, being more than 96% identical to the human counterpart (not shown).…”

Section: Regulation Of Slit Expressionmentioning

confidence: 99%

TheDrosophilaARF6-GEF Schizo controls commissure formation by regulating Slit

2004

View full text Add to dashboard Cite

The CNS of bilateral symmetric organisms is characterized by intensive contralateral axonal connections. Genetic screens in Drosophila have identified only a few genes required for guiding commissural growth cones toward and across the midline. Two evolutionarily conserved signaling molecules, Netrin and Slit, are expressed in the CNS midline cells. Netrin acts primarily as an attractive signaling cue, whereas Slit mediates repulsive functions. Here, we describe a detailed analysis of the Drosophilagene schizo, which is required for commissure formation. schizo leads to a commissural phenotype reminiscent of netrin mutant embryos. Double-mutant analyses indicate that Netrin and Schizo act independently. The schizo mutant phenotype can be suppressed by either expressing netrin in the CNS midline cells or by a reduction of the slit gene dose, indicating that the balance of attractive and repulsive signaling is impaired in schizo mutants. Overexpression of the schizo RNA in the CNS midline using the GAL4/UAS system leads to a slit phenocopy, suggesting that schizo primarily antagonizes Slit signaling. This is further supported by cell type-specific rescue experiments. The schizo gene generates at least two proteins containing a conserved Sec7 and a pleckstrin homology domain (PH) characteristic for guanine nucleotide exchange factors(GEF) acting on ARF GTPases, which are known to regulate endocytosis.In support of the notion that schizo regulates Slit expression via endocytosis, we found that block of endocytosis leads to a schizo-like phenotype. We thus propose that the balance of the two signaling cues Netrin and Slit can be regulated, controlling membrane dynamics.

show abstract

Section: Regulation Of Slit Expressionmentioning

confidence: 99%

TheDrosophilaARF6-GEF Schizo controls commissure formation by regulating Slit

2004

View full text Add to dashboard Cite

show abstract

“…A family of ARF GAP proteins, collectively termed centaurins, have been identified, and all possess one or more PH domains and an ARF GAP catalytic domain [39]. The PH domain on centaurin-α1 interacts with PtdIns(3,4,5)P $ , and centaurin-α1 is recruited to cell membranes after PI 3-kinase is activated [8].…”

Section: Figure 6 Amino Acid Sequence and Tissue Distribution Of Pepp1mentioning

confidence: 99%

Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities

et al. 2000

View full text Add to dashboard Cite

“…No step in membrane traffic specifically requiring Arf4 or -5 has been reported. A number of the guanine nucleotide exchange factors (GEFs) and GTPase accelerating proteins (GAPs) for Arfs, as well as other proteins involved in Golgi membrane traffic, bind PtdIns(4,5)P 2 or PA (30,174,215,265,284,285). Arf1 is a direct activator of both PIP5KIB and PI4KII␤ and stimulates the production of PtdIns(4,5)P 2 on Golgi membranes in vitro (120,168).…”

Section: E Ptdins(4)p and Ptdins(45)p 2 On The Golgimentioning

confidence: 99%

Phosphoinositides in Constitutive Membrane Traffic

Roth

2004

Physiological Reviews

263

267

View full text Add to dashboard Cite

Proteins that make, consume, and bind to phosphoinositides are important for constitutive membrane traffic. Different phosphoinositides are concentrated in different parts of the central vacuolar pathway, with phosphatidylinositol 4-phosphate predominate on Golgi, phosphatidylinositol 4,5-bisphosphate predominate at the plasma membrane, phosphatidylinositol 3-phosphate the major phosphoinositide on early endosomes, and phosphatidylinositol 3,5-bisphosphate found on late endocytic organelles. This spatial segregation may be the mechanism by which the direction of membrane traffic is controlled. Phosphoinositides increase the affinity of membranes for peripheral membrane proteins that function for sorting protein cargo or for the docking and fusion of transport vesicles. This implies that constitutive membrane traffic may be regulated by the mechanisms that control the activity of the enzymes that produce and consume phosphoinositides. Although the lipid kinases and phosphatases that function in constitutive membrane traffic are beginning to be identified, their regulation is poorly understood.

show abstract

The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton

Cited by 203 publications

References 63 publications

TheDrosophilaARF6-GEF Schizo controls commissure formation by regulating Slit

TheDrosophilaARF6-GEF Schizo controls commissure formation by regulating Slit

Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities

Phosphoinositides in Constitutive Membrane Traffic

Contact Info

Product

Resources

About