Tyrosine phosphorylation of tau regulates its interactions
with Fyn SH2 domains, but not SH3 domains, altering the
cellular localization of tau
Alessia Usardi
1
, Amy M. Pooler
1
, Anjan Seereeram
1
, C. Hugh Reynolds
1
, Pascal Derkinderen
1
,
Brian Anderton
1
, Diane P. Hanger
1
, Wendy Noble
1,
* and Ritchie Williamson
1,2,
*
1 Department of Neuroscience, MRC Centre for Neurodegeneration Research, Institute of Psychiatry, King’s College London, UK
2 Biomedical Research Institute, Ninewells Medical School, University of Dundee, UK
Keywords
Fyn-SH2; Fyn-SH3; phosphorylation; tau;
tyrosine
Correspondence
R. Williamson, Biomedical Research
Institute, Ninewells Medical School,

Structured digital abstract
l
Fyn physically interacts with tau by pull down (View interaction)
l
Fyn physically interacts with tau by pull down (View interaction)
Introduction
The microtubule-associated protein tau is a predomi-
nantly neuronal soluble phosphoprotein that is mainly
cytoplasmic, but is also present in nuclear [1,2]
and membrane [3–5] compartments of various cell
types. Abnormalities in tau, including its aberrant
phosphorylation, truncation and aggregation, are
causally associated with neuronal loss in a family of
neurodegenerative disorders named the tauopathies,
which include Alzheimer’s disease (AD), progressive
supranuclear palsy and frontotemporal dementia with
Abbreviations
AD, Alzheimer’s disease; Ab, b-amyloid; CHO, Chinese hamster ovary; CNS, central nervous system; DRM, detergent-resistant
microdomain; GST, glutathione-S-transferase; NMDA, N-methyl-
D-aspartate; PSD, postsynaptic density; SEM, standard error of the mean;
SH, Src homology.
FEBS Journal 278 (2011) 2927–2937 ª 2011 The Authors Journal compilation ª 2011 FEBS 2927
Parkinsonism associated with tau mutations on chro-
mosome 17 [6,7]. In AD, tau is believed to act in syn-
ergy with b-amyloid (Ab) to mediate neuronal loss [8].
Recently, we and others have highlighted the impor-
tance of tau interactions with the membrane-anchored
nonreceptor tyrosine kinase Fyn during A b-mediated
neurodegeneration in cell and animal models of AD
[9–12].

central nervous system (CNS). Two distinct PXXP
motifs in tau, residing within residues 213–219 and
233–236, have been suggested to mediate its associa-
tion with Fyn-SH3 [20,21], and this interaction is regu-
lated by the serine ⁄ threonine phosphorylation status of
tau [21].
Fyn also interacts with proteins through its SH2
domain, which recognizes phosphorylated tyrosines on
target proteins [22,23]. Such interactions regulate the
induction of several signal transduction pathways [24]
that could play a role in Ab-induced neuronal loss.
Tau is known to be tyrosine phosphorylated in post-
mortem AD brain [17,18,25] as well as in transgenic
mouse models of tauopathy, in which tyrosine phos-
phorylated tau is associated with the development of
tau pathology and neuronal loss [26]. Thus, it is
important to establish whether or not tau interacts
with Fyn-SH2, as this would probably reveal that the
tyrosine phosphorylation status of tau is important for
mediating the association of these two proteins.
Here, we used Chinese hamster ovary (CHO) cells to
characterize the interaction between exogenously
expressed human wild-type tau and Fyn. Previous
studies using truncated tau constructs have indicated
that Fyn-SH3 interactions are mediated by either
Pro216 or Pro233 on tau [20,21]. Using mutant forms
of full-length tau, we show that direct interaction with
Fyn-SH3 is mediated predominantly by Pro216 in tau.
In addition, we show that tau interacts with Fyn-SH2
and that tyrosine phosphorylation of tau, particularly

and nonphosphorylated) tau revealed a primary band
of  64 kDa, corresponding to V5-tagged tau, on
western blots of cell lysates (Fig. 1A). Tau was also
detected in the GST–Fyn-SH2-bound fraction, but not
in the GST-only-bound fraction pulldowns (Fig. 1A).
Tyrosine phosphorylation-dependent tau–Fyn binding A. Usardi et al.
2928 FEBS Journal 278 (2011) 2927–2937 ª 2011 The Authors Journal compilation ª 2011 FEBS
This indicates that a proportion of tau interacts with
Fyn-SH2 and that this binding is specific, as it is not
related to the presence of GST. Western blotting with
a polyclonal antibody against GST confirmed that an
equal amount of GST–Fyn-SH2 beads was used in
each pulldown. Pervanadate treatment of CHO cells
coexpressing tau and Fyn resulted in an increased
amount of tau bound to Fyn-SH2, as compared with
cells treated with catalase (Fig. 1A). Furthermore, a
tau species of  68 kDa was apparent in SH2 pull-
downs from pervanadate-treated cells that had been
transfected with tau. This may represent a more highly
phosphorylated tau species or might indicate a differ-
ent conformation of tau with reduced electrophoretic
mobility. Densitometric analysis of GST–Fyn-SH2-
bound tau, as a proportion of total tau in each cell
lysate, revealed that pervanadate increased Fyn-SH2–
tau binding by approximately six-fold as compared
with controls (Fig. 1B). These results show that inhibi-
tion of tyrosine phosphatases with pervanadate results
in significantly increased binding of tau to Fyn-SH2,
thus suggesting that the interaction between tau and
Fyn-SH2 is enhanced by increased tyrosine phosphory-

results show that prevention of tau tyrosine phosphor-
ylation almost completely ablates the ability of tau to
bind to Fyn-SH2, indicating that this interaction is
dependent on tyrosine phosphorylation of tau. A small
proportion of expressed Y18F, Y29F, Y197F, Y310F
and Y394F tau each bound to Fyn-SH2 under control
conditions, and this binding was elevated with per-
vanadate (Fig. 2A). Notably, Y18F tau appeared to be
less able than Y29F, Y197F, Y310F and Y394F tau to
bind GST–Fyn-SH2, suggesting that phosphorylation
of tau at Tyr18 may be particularly important for its
interaction with Fyn-SH2 (Fig. 2B). Western blotting
with a polyclonal antibody against GST confirmed
that the same amount of GST–Fyn-SH2 beads was
used in each pulldown.
The amount of tau bound to GST–Fyn-SH2 follow-
ing pervanadate treatment was quantified as a propor-
tion of tau in cell lysates (Fig. 2B). These results
revealed that tau binding to Fyn-SH2 was almost com-
pletely ablated when all tyrosines on tau were substi-
tuted (YallF). In contrast, all of the tau mutants with
substitutions of individual tyrosines were able to bind
GST–Fyn-SH2 to some extent. Y18F tau showed
Fig. 1. Tyrosine phosphorylation of tau increases its association
with Fyn-SH2. CHO cells were cotransfected with plasmids
expressing Fyn and V5-tagged wild-type tau. Cells were treated
with 100 l
M pervanadate (P) or catalase (C). (A) CHO cell lysates
and proteins pulled down by GST or GST–Fyn-SH2 beads on wes-
tern blots labelled with antibodies against tau (V5) or GST. Num-

was no significant difference in the amount of Y394F
that cosedimented with GST–Fyn-SH2 when compared
with wild-type tau. This may be possible because,
although Fyn-SH2 binds directly to phosphotyro-
sines, the amino acid sequence context of the phosp-
hotyrosine site is also important in SH2 domain
recognition, a property that allows SH2 domains to
display binding preferences for specific sites on target
proteins [28].
Tyrosine phosphorylation does not modulate tau
binding to Fyn-SH3
We and others have previously demonstrated that Fyn
binds to tau predominantly through its SH3 domain,
and this interaction is regulated by serine ⁄ threonine
phosphorylation of tau [20,21]. To determine whether
the tyrosine phosphorylation status of tau also affects
the binding of tau to Fyn-SH3, CHO cells were
cotransfected with Fyn together with either wild-type
or the YF mutant forms of tau. Cell lysates containing
equal amounts of tau were subjected to pulldown
assays with GST–Fyn-SH3, and GST-bound proteins
were then assessed by immunoblotting.
Western blotting of lysates from pervanadate-treated
cells with an antibody against total tau revealed
decreased electrophoretic mobility of tau, with the
appearance of an  68-kDa tau species in wild-type and
all of the mutant forms of tau except for YallF and
Y394F tau (Fig. 3). In contrast to the results obtained
with Fyn-SH2, wild-type tau and all of the YF mutant
tau proteins were detected following pulldown with

suggests that different, and possibly independent, mech-
anisms are involved in these interactions of tau with the
same protein.
Interactions with Fyn-SH3 are regulated by key
PXXP motifs in tau
Tau has been shown to bind Fyn-SH3 through spe-
cific PXXP motifs, seven of which are present in
tau. Six of these occur as three pairs of partially over-
lapping tandem sequences (tau residues Pro176–
Pro182, Pro200–Pro206 and Pro213–Pro219), and the
seventh exists as a separate motif at Pro233–Pro236.
However, there is some discrepancy over which of
these PXXP motifs is most important for tau binding
to Fyn-SH3. In neuroblastoma cells, truncated tau
mutants lacking Pro233–Pro236 were used to demon-
strate that this region of tau is critical for the binding
of tau to Fyn-SH3 [20]. Conversely, using synthetic
peptides, we found that Fyn binds strongly to Pro213–
Pro219 of tau, but exhibits little interaction with
Pro233–Pro236 [21]. To further investigate which
PXXP motifs in tau are responsible for Fyn-SH3
binding, we generated alanine-substituted tau mutant
constructs, P216A and P233A, for V5-tagged wild-type
human tau.
CHO cells were cotransfected with Fyn together
with V5-tagged wild-type, P216A mutant or P233A
mutant tau. Cell lysates were analysed on western blots
probed with an antibody against V5 to confirm the
equivalence of tau protein expression in CHO cells
(Fig. 4A). GST–Fyn-SH3 beads were used to pull

collected, and DRMs were isolated and concentrated.
Western blotting with an antibody against the DRM
marker flotillin-1 was used to demonstrate that DRMs
were successfully isolated from wild-type and Fyn-defi-
cient mice (Fig. 5). Similarly, immunoblotting with an
antibody against Fyn revealed its enrichment in DRMs
prepared from wild-type neurons, but not from neu-
rons lacking Fyn. Increased protein tyrosine phosphor-
ylation following pervanadate treatment of wild-type
Fig. 4. Pro216 in tau is important for its interaction with Fyn-SH3.
CHO cells were transiently cotransfected with Fyn and V5-tagged
wild-type (WT) or mutant P216A or P233A tau. (A) CHO cell lysates
and proteins pulled down by GST–Fyn-SH3 beads were probed
with antibodies against tau (V5) and GST. Numbers on the left indi-
cate molecular masses (kDa). (B) Bar chart showing the proportion
of total tau pulled down by GST–Fyn-SH3 beads. Values shown are
mean fold change from control ± SEM. N =6.*P < 0.05.
A. Usardi et al. Tyrosine phosphorylation-dependent tau–Fyn binding
FEBS Journal 278 (2011) 2927–2937 ª 2011 The Authors Journal compilation ª 2011 FEBS 2931
and Fyn-deficient neuronal cultures was detected with
the phosphotyrosine antibody 4G10 (Fig. 5). There
was no apparent decrease in 4G10 immunoreactivity in
homogenates from Fyn-deficient neurons, and this
probably reflects compensation for the loss of Fyn by
other Src family kinases, as has been previously dem-
onstrated [29].
A tau species of  50–55 kDa, corresponding to
endogenous mouse tau, was detected in lysates and
DRMs isolated from vehicle-treated wild-type and
Fyn-deficient neurons, confirming our previous find-

tial therapeutic strategy for the treatment of AD. Here,
we used GST fusion proteins of Fyn-SH2 and Fyn-
SH3 to further investigate the mechanisms by which
tau and Fyn interact. We determined that tau binds to
both Fyn-SH2 and Fyn-SH3, and only the former of
these associations is mediated by tyrosine phosphoryla-
tion. With the methods employed here, it was not pos-
sible to accurately quantify differences in the relative
proportions of tau capable of binding to Fyn-SH2 and
Fyn-SH3, as there may be variations in the affinity of
Fyn-SH2 and Fyn-SH3 for GST beads. However, our
data suggest that several-fold more tau binds to Fyn-
SH3 than to Fyn-SH2.
Tau binds predominantly to Fyn-SH3, which has a
specific affinity for PXXP motifs in proteins [20,21].
Tau binding to SH3 domains is regulated by the phos-
phorylation of tau on specific serine⁄ threonine residues
[21], and we show here that Fyn-SH3–tau interactions
are not influenced by the tyrosine phosphorylation sta-
tus of tau. Using specific tau constructs in which either
Pro216 or Pro233 was mutated to disrupt critical
PXXP motifs implicated in Fyn binding, we have
shown that Pro216 is especially important for the
interaction of tau with Fyn-SH3, in line with our pre-
vious work [21]. These findings, however, contrast with
those of a previous study in which a deletion mutant
of tau lacking residues 169–179 displayed a 90%
reduction in its binding to Fyn-SH3 [20]. The reason
for this discrepancy is unclear; however, it is possible
that the deletion mutants of tau used previously may

[20]. We therefore conclude that Pro216 in tau plays
an important role in its binding to Fyn-SH3. However,
tau possesses seven PXXP motifs, five of which have
not been investigated, and we therefore cannot exclude
the possibility that other prolines in tau may be impor-
tant for its binding to Fyn-SH3.
Here, we have demonstrated, for the first time, that
tau interacts with Fyn-SH2. Proteins harbouring SH2
domains bind to phosphorylated tyrosines on their tar-
get proteins, thereby coupling the activity of tyrosine
kinases with intracellular signalling pathways [28]. In
our model system, in which exogenous tau and Fyn
were expressed in non-neuronal cells, we found that
only a small proportion of tau is associated with Fyn-
SH2, both under control conditions and following per-
vanadate treatment to induce tyrosine phosphoryla-
tion. The magnitude of the increased tyrosine
phosphorylation that we observed following pervana-
date treatment is similar to that observed following
treatment of cells with physiological amounts of Ab
[30], and thus appears to have physiological relevance.
The influence of this relatively small pool of Fyn-SH2-
bound tau on potential neuronal responses to neuro-
toxic insults such as Ab remains to be determined. The
use of mutant tau constructs in which individual tyro-
sines were mutated to phenylalanine allowed us to
demonstrate that the tyrosine phosphorylation status
of tau significantly influences its ability to bind Fyn-
SH2. Indeed, we determined that Tyr18, the tau resi-
due apparently preferred by Fyn [14,17,18], plays a

could potentially modulate complex formation, and
result in altered trafficking into neuronal membrane
compartments.
In summary, the results presented here suggest that
tyrosine phosphorylation mediates the association of
tau with Fyn-SH2, but not with Fyn-SH3. This dem-
onstrates that different molecular mechanisms exist for
these two distinct interactions of Fyn and tau, with
probably disparate downstream consequences. Further-
more, these results support the view that non-micro-
tubule associations of tau are important for normal
physiological function in neurons, and reinforce the
suggestion that tau is itself involved in intracellular sig-
nalling pathways ⁄ mechanisms. As its interaction with
Fyn is important for tau localization in neurons, regu-
lation of the cellular signalling function of this micro-
tubule-associated protein could also have significant
implications during the progression of neurodegenera-
tive diseases, such as AD, in which both tau and Fyn
are implicated.
Experimental procedures
Plasmids and cell transfection
A plasmid expressing either the longest isoform of human
CNS tau, containing two N-terminal inserts (2N) and four
microtubule-binding repeats (4R), 2N4R tau, was a
generous gift from M. Goedert (Medical Research Council
Laboratory of Molecular Biology, Cambridge, UK) [35].
Generation of 2N4R tau constructs, each with a single tyro-
sine replaced by phenylalanine (Y18F, Y29F, Y197F,
Y310F and Y394F), or all with five tyrosines replaced by

10% (v ⁄ v) fetal bovine serum, 2 m
ML-glutamine, and
100 UÆmL
)1
penicillin ⁄ 100 lgÆmL
)1
streptomycin, and incu-
bated at 37 °Cina5%CO
2
atmosphere. Cells were plated
into six-well dishes and transfected 24 h later by using
Lipofectamine Plus Reagent (Invitrogen), following the
manufacturer’s instructions. Pervandate and catalase were
prepared as described previously [25]. Briefly, vanadate
stock solution was prepared as a 200 m
M solution of
sodium orthovanadate (pH 10). Pervanadate was prepared
as a ·100 stock by adding 50 lL of 200 m
M sodium ortho-
vanadate and 1.6 lL of 30% (w ⁄ w) hydrogen peroxide to
948.4 lL of water for 5 min at room temperature, giving
10 m
M sodium orthovanadate and 16.3 mM hydrogen per-
oxide. After 5 min at room temperature, the excess hydro-
gen peroxide was removed by addition of 200 lgÆmL
)1
catalase (520 UÆmL
)1
) and incubation for an additional
5 min, as described by Huyer et al. [27]. Twenty-four hours

beads washed three times with lysis buffer. Laemmli sample
buffer was added, and the samples were heated to 100 °C
for 5 min to release bound proteins. Proteins in CHO cell
lysates were separated on 10–12% polyacrylamide gels,
transferred to nitrocellulose, and probed with an antibody
to tau. The amount of tau in each sample was quantified
by densitometry, and samples were adjusted by dilution in
lysis buffer to ensure equal tau protein concentrations for
subsequent determination of the relative amounts of GST-
bound proteins.
Animals and culture of primary cortical neurons
Wild-type and Fyn-deficient (Fyn
) ⁄ )
) mice were obtained
from The Jackson Laboratory (Bar Habor, Maine, USA).
Fyn
) ⁄ )
mice were maintained on a mixed B6129F2 ⁄ J back-
ground, and the same strain was used to provide wild-type
controls. All animal work was licensed under the Animals
(Scientific Procedures) Act 1986, reviewed by the ethical
review panel of King’s College London, Institute of Psychia-
try and the Home Office inspectorate, and performed in
accordance with the European Communities Council Direc-
tive of 24 November 1986 (86 ⁄ 609 ⁄ EEC). Primary cortical
neurons were prepared from embryonic day 16 wild-type and
Fyn-deficient mouse embryos, as described previously [9].
Cells were plated onto six-well dishes coated with poly(
D-
lysine) (5 lgÆmL

Dounce homogenizer, and incubated on ice for 30 min.
One millilitre of homogenate was mixed with 1 mL of
90% (w ⁄ v) sucrose in MBS buffer, and placed in a 12-mL
ultracentrifuge tube. A discontinuous 5%–35%–45%
sucrose gradient was formed by layering 6 mL of
35% (w ⁄ v) sucrose in MBS buffer on top of the 2-mL
homogenate, followed by 4 mL of 5% (w ⁄ v) sucrose in
MBS buffer. Samples were centrifuged at 180 000 g for
18 h at 4 °C in a Beckman SW41 rotor (Beckman Instru-
ments, Fullerton, CA, USA). Twelve 1-mL fractions were
collected from the top of each gradient. To concentrate
DRMs in fractions 4–5, 10 mL of MBS buffer was added
and the samples were centrifuged at 110 000 g for 1 h at
4 °C in a Beckman SW41 rotor. The resulting pellet was
solubilized in 100 lLof20m
M Tris ⁄ HCl (pH 7.4) contain-
ing 8
M urea, 10 mM NaF, 2 mM Na
3
VO
4
and 5 mM dith-
iothreitol. Samples were mixed with Laemlli buffer and
heated at 100 °C for 5 min prior to analysis by SDS ⁄
PAGE.
SDS
⁄
PAGE and western blotting
Denaturing PAGE and western blotting were performed as
described previously [37]. Briefly, separated proteins were

error of the mean (SEM).
Acknowledgements
We thank the following for gifts of materials: M.
Goedert (MRC Laboratory of Molecular Biology,
Cambridge, UK) for tau 2N4R cDNA; S. Anderson
(University of Colorado Health Sciences Center) for
pGEX constructs; and D. Markby (Sugen, San Fran-
cisco, CA, USA) for human Fyn cDNA. This work
was supported by Alzheimer’s Research UK, the Alz-
heimer’s Society, and the Medical Research Council.
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