Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin
Schüler, Herwig LU
and Peti, Wolfgang
(2008)
In The FEBS Journal
275(1).
p.59-68
- Abstract
Spinophilin, a neuronal scaffolding protein, is essential for synaptic transmission, and functions to target protein phosphatase-1 to distinct subcellular locations in dendritic spines. It is vital for the regulation of dendritic spine formation and motility, and functions by regulating glutamatergic receptors and binding to filamentous actin. To investigate its role in regulating actin cytoskeletal structure, we initiated structural studies of the actin binding domain of spinophilin. We demonstrate that the spinophilin actin binding domain is intrinsically unstructured, and that, with increasing C-terminal length, the domain shows augmented secondary structure content. Further characterization confirmed the previously known... (More)
Spinophilin, a neuronal scaffolding protein, is essential for synaptic transmission, and functions to target protein phosphatase-1 to distinct subcellular locations in dendritic spines. It is vital for the regulation of dendritic spine formation and motility, and functions by regulating glutamatergic receptors and binding to filamentous actin. To investigate its role in regulating actin cytoskeletal structure, we initiated structural studies of the actin binding domain of spinophilin. We demonstrate that the spinophilin actin binding domain is intrinsically unstructured, and that, with increasing C-terminal length, the domain shows augmented secondary structure content. Further characterization confirmed the previously known crosslinking activity and uncovered a novel filamentous actin pointed-end capping activity. Both of these functions seem to be fully contained within residues 1-154 of spinophilin.
(Less)
- author
- Schüler, Herwig
LU
and Peti, Wolfgang
- publishing date
- 2008-01
- type
- Contribution to journal
- publication status
- published
- keywords
- Animals, Circular Dichroism, Cloning, Molecular, Microfilament Proteins/chemistry, Nerve Tissue Proteins/chemistry, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Protein Structure, Tertiary, Rats, Structure-Activity Relationship
- in
- The FEBS Journal
- volume
- 275
- issue
- 1
- pages
- 10 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:37349112080
- pmid:18028445
- ISSN
- 1742-464X
- DOI
- 10.1111/j.1742-4658.2007.06171.x
- language
- English
- LU publication?
- no
- id
- aaf8240a-2619-43ae-bb50-8d06481cb85d
- date added to LUP
- 2024-11-21 18:04:46
- date last changed
- 2025-01-03 07:48:14
@article{aaf8240a-2619-43ae-bb50-8d06481cb85d,
abstract = {{<p>Spinophilin, a neuronal scaffolding protein, is essential for synaptic transmission, and functions to target protein phosphatase-1 to distinct subcellular locations in dendritic spines. It is vital for the regulation of dendritic spine formation and motility, and functions by regulating glutamatergic receptors and binding to filamentous actin. To investigate its role in regulating actin cytoskeletal structure, we initiated structural studies of the actin binding domain of spinophilin. We demonstrate that the spinophilin actin binding domain is intrinsically unstructured, and that, with increasing C-terminal length, the domain shows augmented secondary structure content. Further characterization confirmed the previously known crosslinking activity and uncovered a novel filamentous actin pointed-end capping activity. Both of these functions seem to be fully contained within residues 1-154 of spinophilin.</p>}},
author = {{Schüler, Herwig and Peti, Wolfgang}},
issn = {{1742-464X}},
keywords = {{Animals; Circular Dichroism; Cloning, Molecular; Microfilament Proteins/chemistry; Nerve Tissue Proteins/chemistry; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Structure-Activity Relationship}},
language = {{eng}},
number = {{1}},
pages = {{59--68}},
publisher = {{John Wiley & Sons Inc.}},
series = {{The FEBS Journal}},
title = {{Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin}},
url = {{http://dx.doi.org/10.1111/j.1742-4658.2007.06171.x}},
doi = {{10.1111/j.1742-4658.2007.06171.x}},
volume = {{275}},
year = {{2008}},
}