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Low SPIN90 expression is associated with Breast Cancer.
findings suggest that SPIN90 contributes to the formation and movement of endosomal vesicles, and modulates the stability of EGFR protein, which affects cell cycle progression
SPIN90 dephosphorylation is a prerequisite step for releasing cofilin so that cofilin can adequately sever actin filaments into monomeric form.
Findings show that SPIN90 modulates synaptic activity in neurons as a result of its phosphorylation.
Dia2 and DIP co-tether to nascent blebs and this linkage is required for bleb formation.
the interaction of the betaPIX.WASP.SPIN90 complex with Nck is crucial for stable cell adhesion and can be dynamically modulated by SPIN90 phosphorylation that is dependent on cell adhesion and ERK activation
SPIN90 participates in reorganization of the actin cytoskeleton and in actin-based cell motility
DIP binds to and inhibits actin assembly by the FH2 domain of the formin mDia2
The interplay between palladin, SPIN90 and Src and characterized the role of palladin and SPIN90 in platelet derived growth factor and Src-induced cytoskeletal remodeling, was analyzed.
SPIN90 and IRSp53 positively cooperated to mediate Rac activation, and co-expression of SPIN90 and IRSp53 in COS-7 cells led to the complex formation of SPIN90-IRSp53 in the leading edge of cells
Data suggest that Src homology 3 (SH3) protein interacting with NcK, 90 kDa (SPIN90)plays an important role in B cell immune responses through the regulation of chemokine CXCL13-mediated B cell migration.
DIP/WISH deletion improves performance in the Barnes maze test in mice probably through increased hippocampal long-term potentiation.
SPIN90 plays critical roles in controlling growth cone dynamics and neurite outgrowth during neuronal development.
Results show that DIP/WISH binds to mammalian diaphanous and N-WASP, and functions as a scaffold protein by binding to Nck protein.
identification of a new interaction between Nef and diaphanous interacting protein (DIP), a recently described regulator of Rho and Rac signaling
SPIN90 is a Shank1b binding partner and a key contributor to the regulation of dendritic spine morphogenesis and brain function
The protein encoded by this gene is localized exclusively in the cell nucleus. It plays a role in signal transduction, and may function in the maintenance of sarcomeres and in the assembly of myofibrils into sarcomeres. It also plays an important role in stress fiber formation. The gene is involved in therapy-related leukemia by a chromosomal translocation t(3\;11)(p21\;q23) that involves this gene and the myeloid/lymphoid leukemia gene. Alternative splicing occurs in this locus and two transcript variants encoding distinct isoforms have been identified.
SH3 adapter protein SPIN90
, 54 kDa VacA-interacting protein
, 54 kDa vimentin-interacting protein
, 90 kDa SH3 protein interacting with Nck
, NCK-interacting protein with SH3 domain
, SH3 protein interacting with Nck, 90 kDa
, WASP-interacting SH3-domain protein
, dia interacting protein
, dia-interacting protein 1
, diaphanous protein interacting protein
, wiskott-Aldrich syndrome protein-interacting protein
, 90 kDa N-WASP-interacting protein
, N-WASP-binding protein
, Wiskott-Aldrich syndrome homolog binding protein
, mDia interacting protein-1
, wiskott-Aldrich syndrome protein-binding protein WISH