Abstract
Synapsin I is a neuron-specific phosphoprotein which binds to small synaptic vesicles and actin in a phosphorylation-dependent fashion. We have analyzed the ability of synapsin I to interact with actin monomers and filaments using purified proteins derivatized with fluorescent probes. Synapsin I accelerates the initial rate of actin polymerization and increases the final steady-state levels of polymerized actin. The fraction of total actin polymerized by synapsin I strongly depends on the synapsin I-actin ratio. We have visualized the actin-bundling activity of synapsin I using a non-perturbing method, video-enhanced microscopy of fluoresceinated synapsin I and actin filaments. Our findings suggest that synapsin I exerts a control on the physical characteristics of the cytoskeletal network of the nerve terminal and are consistent with the proposed role of synapsin I in mediating the interaction of synaptic vesicles with actin.
| Original language | English |
|---|---|
| Pages (from-to) | 117-122 |
| Number of pages | 6 |
| Journal | Journal of Physiology Paris |
| Volume | 87 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1993 |
Fingerprint
Keywords
- actin polymerization
- protein phosphorylation
- pyrenyl-actin
- synaptic vesicles
ASJC Scopus subject areas
- Physiology (medical)
- Neuroscience(all)
Cite this
Fluorescence approaches to the study of the actin-nucleating and bundling activities of synapsin I. / Valtorta, F.; Ceccaldi, P. E.; Grohovaz, F.; Chieregatti, E.; Fesce, R.; Benfenati, F.
In: Journal of Physiology Paris, Vol. 87, No. 2, 1993, p. 117-122.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Fluorescence approaches to the study of the actin-nucleating and bundling activities of synapsin I
AU - Valtorta, F.
AU - Ceccaldi, P. E.
AU - Grohovaz, F.
AU - Chieregatti, E.
AU - Fesce, R.
AU - Benfenati, F.
PY - 1993
Y1 - 1993
N2 - Synapsin I is a neuron-specific phosphoprotein which binds to small synaptic vesicles and actin in a phosphorylation-dependent fashion. We have analyzed the ability of synapsin I to interact with actin monomers and filaments using purified proteins derivatized with fluorescent probes. Synapsin I accelerates the initial rate of actin polymerization and increases the final steady-state levels of polymerized actin. The fraction of total actin polymerized by synapsin I strongly depends on the synapsin I-actin ratio. We have visualized the actin-bundling activity of synapsin I using a non-perturbing method, video-enhanced microscopy of fluoresceinated synapsin I and actin filaments. Our findings suggest that synapsin I exerts a control on the physical characteristics of the cytoskeletal network of the nerve terminal and are consistent with the proposed role of synapsin I in mediating the interaction of synaptic vesicles with actin.
AB - Synapsin I is a neuron-specific phosphoprotein which binds to small synaptic vesicles and actin in a phosphorylation-dependent fashion. We have analyzed the ability of synapsin I to interact with actin monomers and filaments using purified proteins derivatized with fluorescent probes. Synapsin I accelerates the initial rate of actin polymerization and increases the final steady-state levels of polymerized actin. The fraction of total actin polymerized by synapsin I strongly depends on the synapsin I-actin ratio. We have visualized the actin-bundling activity of synapsin I using a non-perturbing method, video-enhanced microscopy of fluoresceinated synapsin I and actin filaments. Our findings suggest that synapsin I exerts a control on the physical characteristics of the cytoskeletal network of the nerve terminal and are consistent with the proposed role of synapsin I in mediating the interaction of synaptic vesicles with actin.
KW - actin polymerization
KW - protein phosphorylation
KW - pyrenyl-actin
KW - synaptic vesicles
UR - http://www.scopus.com/inward/record.url?scp=0027216334&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027216334&partnerID=8YFLogxK
U2 - 10.1016/0928-4257(93)90005-E
DO - 10.1016/0928-4257(93)90005-E
M3 - Article
VL - 87
SP - 117
EP - 122
JO - Journal de Physiologie
JF - Journal de Physiologie
SN - 0928-4257
IS - 2
ER -