Editing Reelin (section)

=== Complexes ===
Reelin molecules have been shown<ref name="hugecomplex" /><ref name="complex" /> to form a large protein complex, a [[disulfide bond|disulfide-linked]] [[homodimer]]. If the homodimer fails to form, efficient tyrosine [[phosphorylation]] of DAB1 ''in vitro'' fails. Moreover, the two main receptors of reelin are able to form clusters<ref name="pmid14729980" /> that most probably play a major role in the signaling, causing the intracellular adaptor DAB1 to dimerize or oligomerize in its turn. Such clustering has been shown in the study to activate the signaling chain even in the absence of Reelin itself.<ref name="pmid14729980" /> In addition, reelin itself can cut the peptide bonds holding other proteins together, being a [[serine protease]],<ref name="pmid11689558" /> and this may affect the cellular adhesion and migration processes. Reelin signaling leads to phosphorylation of [[actin]]-interacting protein [[cofilin 1]] at ser3; this may stabilize the actin cytoskeleton and anchor the leading processes of migrating neuroblasts, preventing their further growth.<ref name="pmid19129405" /><ref name="pmid19396394" />