RAPID BINDING OF SYNAPSIN-I TO F-ACTIN AND G-ACTIN - A STUDY USING FLUORESCENCE RESONANCE ENERGY-TRANSFER

被引：16

作者：

CECCALDI, PE

BENFENATI, F

CHIEREGATTI, E

GREENGARD, P

VALTORTA, F

机构：

[1] UNIV MILAN,S RAFFAELE SCI INST,DIBIT,NEUROBIOL UNIT,VIA OLGETTINA 60,I-20132 MILAN,ITALY

[2] UNIV MILAN,CNR,B CECCARELLI CTR,CTR CYTOPHARMACOL,DEPT MED PHARMACOL,I-20132 MILAN,ITALY

[3] UNIV MODENA,INST HUMAN PHYSIOL,I-41100 MODENA,ITALY

[4] UNIV ROMA TOR VERGATA,DEPT EXPTL MED,ROME,ITALY

[5] ROCKEFELLER UNIV,NEW YORK,NY 10021

来源：

FEBS LETTERS | 1993年 / 329卷 / 03期

关键词：

SYNAPTIC VESICLE; NERVE TERMINAL; PROTEIN PHOSPHORYLATION;

D O I：

10.1016/0014-5793(93)80242-M

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Synapsin I is a nerve terminal phosphoprotein which interacts with synaptic vesicles and actin in a phosphorylation-dependent manner. By using fluorescence resonance energy transfer between purified components labeled with fluorescent probes, we now show that the binding of synapsin I to actin is a rapid phenomenon. Binding of synapsin I to actin can also be demonstrated when synaptic vesicles are present in the medium and appears to be modulated by ionic strength and synapsin I phosphorylation.

引用

页码：301 / 305

页数：5

共 19 条

[1] SYNAPSIN-I BUNDLES F-ACTIN IN A PHOSPHORYLATION-DEPENDENT MANNER [J].