For this review we will focus the discussion mainly on vimentin, as vimentin is one of the best investigated intermediate laments.Notably, we will not discuss keratins, as they are mostly restricted to epithelial cells and keratinocytes and not present in cell of glial origin.In nonmigrating cells intermediate laments are mostly Dutasteride localized around the nucleus, extending into the periphery, while they elongate into the lamella, connecting to focal adhesions near the leading edge in migrating cells. In the lamellipodium intermediate laments are found mostly in a nonlamentous state. Generally speaking, intermediate lament organization alters the current state of the two other cytoskeletal components, thus potentially modulating both cell adhesion and migration.A strong hint for intermediate laments inuencing cell migration comes from the observation that, for example, vimentin can interact with actin and neurolaments with microtubules, epithelial cell wound closure. Vimentin inhibition reduces motility in broblasts, astrocytes, and diverse cancer cells. Studies evaluating possible mechanisms found evidence for vimentin directly binding to APC.APC regulates vimentin organization in astrocytes to align vimentin along the microtubule network. Posttranslational modications, like detyronsination and acetylation of microtubules, also impact vimentin network organization. On the other hand vimentin also aects polarized microtubule organization, amongst others by forming a template for microtubules, guiding microtubule growth, and, thus, favor directed migration. The exact mechanism of this interaction is not yet fully understood but may be governed by APC, linking microtubules and vimentin or via vimentin phosphorylation. Conversely, the vimentin lament network is dependent on microtubules and its motor proteins.Microtubule disruption leads to vimentin relocalization around the nucleus. Another motility associated structure partly regulated by vimentin are focal adhesions.Vimentin is associated with formation, maturation, size, and strength of focal adhesions. Additionally, a triple silencing of vimentin, GFAP, and nestin or of vimentin and GFAP in astrocytes demonstrated that these intermediate laments help to maintain the polarization of leader cells in collective motion by controlling forces in monolayers. Silencing of each individual intermediate lament produced similar but less pronounced results. This eect was attributed to larger and more focal adhesions that were distributed less concentratedly at the cell front. It is supposed that those three intermediate laments control focal adhesions and traction force in astrocytes via plectin to control vinculin recruitment. A further hypothesis of how intermediate laments control focal adhesions and traction forces is via the actomyosin network, by redirecting forces and restraining actin retrograde ow. In line with these ndings, Dicyclomine hydrochloride transverse arcs interact via plectin with vimentin to promote their retrograde ow and this coupling is necessary for the perinuclear organization of vimentin laments. Consequently, myosin II driven contractility of transversal arcs was made responsible for retrograde vimentin movement. Conversely, local vimentin depolymerization causes the formation of the lamellipodium at the side of vimentin depletion. Consequently, vimentin coregulates both contractile actomyosin bundles and protrusive lamellipodial actin, and thus cell polarization.Despite the regulation of actin dynamics in the lamellipodium and lamellum, vimentin seems to form a transport structure for the nucleus in a three dimensional environment in cooperation with actomyosin, via the creation of a pressure gradient.