The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain

Article Abstract:

Serum response factor (SRF) interacts with c-fos serum response element (SRE), a sequence mediating the transcriptional response of many cellular genes to growth factor stimuli. SRF, SRE and SRF accessory factor Elk-1 form a ternary complex. Recombinant Elk-1 was treated with phosphatase and MAP kinase to characterize the activity and regulation of SRE-binding proteins. Results showed that MAP kinase phosphorylates the Elk-1 C1 terminal region at multiple sites showing that this region functions as a growth factor-regulated transcriptional activation domain.

Growth factors

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Functional analysis of a growth factor-responsive transcription factor complex

Article Abstract:

Serum response factor (SRF), binds the serum response element (SRE), which is a sequence that mediates the transient transcriptional response of many cellular genes to growth factor stimulation. Functional analysis of the ternary complex that is composed of SRF, SRE and accessory factor Elk-1 was done using altered binding specificity derivatives of SRF and Elk-1. Results showed that regulated phosphorylation of Elk-1 C-terminal MAP kinase sites and C-terminal sequence of SRF are required for efficient transcriptional activation.

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The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF

Article Abstract:

The three Rho family GTPases RhoA, Rac1 and CDC42Hs, help in the activity of c-fos, a serum response element (SRE) to form ternary complex by two transcription factors, serum response factor (SRF) and ternary complex factor (TCF). SRF transcripts when induced by serum, lysophosphatidic acid or intracellular activation of heterotrimeric G protein. SRF-linked signaling pathway is a unique activation target, separate from MAP kinase ERK, SAPK\JNK, or MPK2\p38.

Analysis, G proteins

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